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EC Number Crystallization (Commentary)
Show all pathways known for 1.14.14.14Display the word mapDisplay the reaction diagram Show all sequences 1.14.14.14free energy simulations of the entry/exit routes preferentially followed by substrate androstenedione and inhibitor letrozole. Two channels appear accessible to their entrance, while only one exit route appears to be preferential, ligand channeling is associated with large enzyme structural rearrangements
Show all pathways known for 1.14.14.14Display the word mapDisplay the reaction diagram Show all sequences 1.14.14.14molecular docking studies with inhibitors based on PDB entry 3EQM. The 2-arylindoles prefer binding with the 2-aryl group toward a small hydrophobic pocket within the active site. The C-5 electron withdrawing group on indole may have an important role and form a hydrogen bond with Ser478 (OH). Meta-pyridyl analogs may orient with the pyridyl 3'-nitrogen coordinating with the heme group
Show all pathways known for 1.14.14.14Display the word mapDisplay the reaction diagram Show all sequences 1.14.14.14molecular dynamics simulations of the dimeric interfaces, i.e.residues 45-496
Show all pathways known for 1.14.14.14Display the word mapDisplay the reaction diagram Show all sequences 1.14.14.14molecular modeling of structure
Show all pathways known for 1.14.14.14Display the word mapDisplay the reaction diagram Show all sequences 1.14.14.14to 1.8 A resolution, in complex with its natural substrate androst-4-ene-3,17-dione. Aromatase has an androgen-specific cleft that binds the androstenedione molecule snugly. Hydrophobic and polar residues complement the steroid backbone
Results 1 - 5 of 5