2JJN
Structure of closed cytochrome P450 EryK
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0006707 | biological_process | cholesterol catabolic process |
| A | 0008395 | molecular_function | steroid hydroxylase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| A | 0016709 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen |
| A | 0017000 | biological_process | antibiotic biosynthetic process |
| A | 0020037 | molecular_function | heme binding |
| A | 0033068 | biological_process | macrolide biosynthetic process |
| A | 0036199 | molecular_function | cholest-4-en-3-one 26-monooxygenase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050661 | molecular_function | NADP binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE HEM A 412 |
| Chain | Residue |
| A | ILE87 |
| A | THR246 |
| A | LEU249 |
| A | MET291 |
| A | ARG293 |
| A | SER345 |
| A | PHE346 |
| A | GLY347 |
| A | HIS351 |
| A | CYS353 |
| A | GLY355 |
| A | HIS88 |
| A | LEU358 |
| A | ALA359 |
| A | HOH2131 |
| A | HOH2537 |
| A | HOH2538 |
| A | HOH2539 |
| A | HIS95 |
| A | ARG99 |
| A | PHE106 |
| A | LEU238 |
| A | ALA241 |
| A | GLY242 |
| A | THR245 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 413 |
| Chain | Residue |
| A | ARG381 |
| A | ARG385 |
| A | LEU386 |
| A | HIS388 |
| A | HOH2540 |
| A | HOH2541 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 414 |
| Chain | Residue |
| A | HIS326 |
| A | ASP327 |
| A | ARG336 |
| A | SER338 |
| A | HOH2542 |
| A | HOH2543 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 415 |
| Chain | Residue |
| A | ARG55 |
| A | HOH2424 |
| A | HOH2544 |
| A | HOH2545 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 416 |
| Chain | Residue |
| A | ARG99 |
| A | SER103 |
| A | LEU354 |
| A | HOH2546 |
| A | HOH2547 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 A 417 |
| Chain | Residue |
| A | HIS56 |
| A | HIS326 |
| A | ALA342 |
| A | LEU344 |
| A | HOH2434 |
| A | HOH2464 |
| A | HOH2548 |
| A | HOH2549 |
| A | HOH2550 |
| A | HOH2551 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGhGVHFCLG |
| Chain | Residue | Details |
| A | PHE346-GLY355 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | HIS88 | |
| A | HIS95 | |
| A | ARG99 | |
| A | GLN292 | |
| A | ARG293 | |
| A | HIS351 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: axial binding residue |
| Chain | Residue | Details |
| A | CYS353 |
