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Ligand 6-hydroxyuridine 5'-phosphate
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Basic Ligand Information
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open all tablesRoles as Enzyme Ligand
Product in Enzyme-catalyzed Reactions (49 results)
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EC NUMBER 
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
Inhibitor in Enzyme-catalyzed Reactions (245 results)
EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
3D Structure of Enzyme-Ligand-Complex (PDB) (104 results)
EC NUMBER
ENZYME 3D STRUCTURE
Enzyme Kinetic Parameters
Ki Value (3 results)
EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
References & Links
Literature References (5)
Links to other databases for 6-hydroxyuridine 5'-phosphate
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