6T0K
Crystal structure of CYP124 in complex with inhibitor carbethoxyhexyl imidazole
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006631 | biological_process | fatty acid metabolic process |
| A | 0006707 | biological_process | cholesterol catabolic process |
| A | 0008395 | molecular_function | steroid hydroxylase activity |
| A | 0010430 | biological_process | fatty acid omega-oxidation |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| A | 0020037 | molecular_function | heme binding |
| A | 0031073 | molecular_function | cholesterol 26-hydroxylase activity |
| A | 0036199 | molecular_function | cholest-4-en-3-one 26-monooxygenase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070402 | molecular_function | NADPH binding |
| A | 0097089 | biological_process | methyl-branched fatty acid metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | binding site for residue HEM A 501 |
| Chain | Residue |
| A | MET110 |
| A | PRO314 |
| A | VAL315 |
| A | ARG320 |
| A | TYR343 |
| A | GLY370 |
| A | PHE371 |
| A | GLY372 |
| A | HIS377 |
| A | CYS379 |
| A | GLY381 |
| A | ILE111 |
| A | M65502 |
| A | HOH662 |
| A | HOH737 |
| A | HOH801 |
| A | HOH839 |
| A | HIS118 |
| A | ARG122 |
| A | LEU264 |
| A | ALA267 |
| A | GLY268 |
| A | THR271 |
| A | THR272 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue M65 A 502 |
| Chain | Residue |
| A | PHE107 |
| A | ILE197 |
| A | VAL266 |
| A | ALA267 |
| A | THR271 |
| A | HEM501 |
| A | GOL504 |
| A | HOH472 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 503 |
| Chain | Residue |
| A | TRP294 |
| A | ARG397 |
| A | HOH884 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 504 |
| Chain | Residue |
| A | ASN93 |
| A | THR95 |
| A | ASN97 |
| A | GLN99 |
| A | PHE107 |
| A | M65502 |
| A | GOL506 |
| A | HOH472 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | binding site for residue GOL A 505 |
| Chain | Residue |
| A | ASP36 |
| A | ASP40 |
| A | HIS278 |
| A | ARG285 |
| A | TRP311 |
| A | HIS418 |
| A | CL509 |
| A | HOH606 |
| A | HOH645 |
| A | HOH840 |
| A | HOH878 |
| A | HOH1114 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | binding site for residue GOL A 506 |
| Chain | Residue |
| A | PHE63 |
| A | THR95 |
| A | ILE197 |
| A | LEU198 |
| A | PHE200 |
| A | PHE416 |
| A | GOL504 |
| A | HOH642 |
| A | HOH814 |
| A | HOH831 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 507 |
| Chain | Residue |
| A | HOH678 |
| A | HOH799 |
| A | HOH1087 |
| A | HOH1104 |
| A | HOH1239 |
| A | HOH1260 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 508 |
| Chain | Residue |
| A | HOH661 |
| A | HOH803 |
| A | HOH1103 |
| A | HOH1137 |
| A | HOH1183 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue CL A 509 |
| Chain | Residue |
| A | ARG285 |
| A | TRP311 |
| A | GOL505 |
| A | HOH699 |
| A | HOH878 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"19933331","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2WM4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WM5","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
