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<< < Results 211 - 215 of 215
EC Number Inhibitors Commentary Structure
Display the word mapDisplay the reaction diagram Show all sequences 5.6.1.3PVZB1194 allosteric inhibitor, biphenyl-type inhibitor, binding structure of the inhibitor in complex with the Eg5 motor domain: inhibitor PVZB1194 binds to the alpha4/alpha6 allosteric pocket 15 A from the ATP-binding pocket, which differs from conventional allosteric inhibitors that bind to the allosteric L5/alpha2/alpha 3 pocket of Eg5. Binding of the inhibitor is involved in the neck-linker conformation and also causes conformational changes around the ATP-binding pocket through Tyr104 to affect the interaction of ATP with the pocket. Folding rearrangement of enzyme Eg5 induced by PVZB1194 in the absence of nucleotides and microtubules. Residue Tyr104 is involved in ATP-competitive inhibition by PVZB1194 Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 5.6.1.3S-trityl-L-cysteine tight binding inhibitor, specific for kinesin Eg5. Inhibits Eg5-driven microtubule sliding velocity in a reversible fashion with a IC50 of 500 nM. The S and D-enantiomers of tritylcysteine are nearly equally potent. No inhibition of KIF2A/Kif2 (kinesin-13 family), KIF2C/MCAK (kinesin-13 family), KIF5B/HsuKHC (kinsin-1 family), KIF19/HsCENP-E (kinesin-7 family), KIF20A/HsRabK6 (kinsin-6 family), KIF22A/HsKid (kinesin-10 family), KIF23/HsMKLP1 (kinesin-6 family), KIFC1/HsKIFC1 (kinesin-14 family) Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 5.6.1.3S-trityl-L-cysteine - Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 5.6.1.3SB-731489 - Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 5.6.1.3V5+ - Go to the Ligand Summary Page
<< < Results 211 - 215 of 215