6T0L
Crystal structure of CYP124 in complex with inhibitor compound 5'
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| 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 | 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 | 22 |
| Details | binding site for residue HEM A 501 |
| Chain | Residue |
| A | ILE111 |
| A | GLY370 |
| A | PHE371 |
| A | GLY372 |
| A | HIS377 |
| A | CYS379 |
| A | LEU380 |
| A | GLY381 |
| A | ALA385 |
| A | M8N502 |
| A | HOH620 |
| A | HIS118 |
| A | HOH652 |
| A | HOH685 |
| A | HOH687 |
| A | ARG122 |
| A | LEU264 |
| A | ALA267 |
| A | GLY268 |
| A | THR271 |
| A | ARG320 |
| A | TYR343 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue M8N A 502 |
| Chain | Residue |
| A | ILE94 |
| A | ILE111 |
| A | VAL266 |
| A | ALA267 |
| A | THR271 |
| A | PHE416 |
| A | ILE417 |
| A | HEM501 |
| A | HOH608 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue PG4 A 503 |
| Chain | Residue |
| A | ALA354 |
| A | ASP355 |
| A | ASP360 |
| A | ALA362 |
| A | ARG363 |
| A | ASN364 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue PEG A 504 |
| Chain | Residue |
| A | ASP77 |
| A | ASP77 |
| A | ARG329 |
| A | ARG329 |
| A | HOH688 |
| A | HOH688 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | binding site for residue PG4 A 505 |
| Chain | Residue |
| A | TRP294 |
| A | LYS332 |
| A | ARG397 |
| A | ARG398 |
| A | HOH603 |
| A | HOH639 |
| A | HOH805 |
| A | HOH813 |
| A | HOH947 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 506 |
| Chain | Residue |
| A | ARG83 |
| A | GLY375 |
| A | ARG398 |
| A | GLN399 |
| A | PRO401 |
| A | HOH626 |
| A | HOH805 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 507 |
| Chain | Residue |
| A | PHE79 |
| A | TYR80 |
| A | HIS84 |
| A | ARG329 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | BINDING: axial binding residue => ECO:0000269|PubMed:19933331, ECO:0007744|PDB:2WM4, ECO:0007744|PDB:2WM5 |
| Chain | Residue | Details |
| A | CYS379 |
