6T0J
Crystal structure of CYP124 in complex with SQ109
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 | ILE111 |
| A | ARG320 |
| A | TYR343 |
| A | GLY370 |
| A | PHE371 |
| A | GLY372 |
| A | HIS377 |
| A | CYS379 |
| A | LEU380 |
| A | GLY381 |
| A | ALA385 |
| A | HIS118 |
| A | RWZ502 |
| A | HOH675 |
| A | HOH749 |
| A | HOH755 |
| A | HOH828 |
| A | ARG122 |
| A | LEU264 |
| A | ALA267 |
| A | GLY268 |
| A | THR271 |
| A | THR272 |
| A | VAL315 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | binding site for residue RWZ A 502 |
| Chain | Residue |
| A | LEU60 |
| A | PHE63 |
| A | THR95 |
| A | ASN97 |
| A | PHE107 |
| A | ILE197 |
| A | LEU198 |
| A | PHE200 |
| A | MET318 |
| A | HEM501 |
| A | HOH879 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 503 |
| Chain | Residue |
| A | ASP355 |
| A | THR358 |
| A | ASP360 |
| A | ARG363 |
| A | HOH643 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 504 |
| Chain | Residue |
| A | PRO92 |
| A | GLN99 |
| A | HOH636 |
| A | HOH1037 |
| A | HOH1246 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | binding site for residue TRS A 505 |
| Chain | Residue |
| A | GLU306 |
| A | ASN366 |
| A | PRO367 |
| A | HIS368 |
| A | PHE371 |
| A | PHE378 |
| A | ARG386 |
| A | HOH843 |
| A | HOH883 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 506 |
| Chain | Residue |
| A | HOH706 |
| A | HOH838 |
| A | HOH1122 |
| A | HOH1174 |
| A | HOH1300 |
| A | HOH1334 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue FMT A 507 |
| Chain | Residue |
| A | GLY13 |
| A | ASP355 |
| A | PRO356 |
| A | TRP357 |
| A | THR358 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue FMT A 508 |
| Chain | Residue |
| A | HOH647 |
| A | HOH699 |
| A | HOH822 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue FMT A 509 |
| Chain | Residue |
| A | GLU327 |
| A | ARG329 |
| A | GLY330 |
| site_id | AD1 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 510 |
| Chain | Residue |
| A | ARG48 |
| A | GLU49 |
| A | PRO51 |
| A | ARG329 |
| A | HOH601 |
| A | HOH634 |
| A | HOH936 |
| A | HOH979 |
| site_id | AD2 |
| Number of Residues | 2 |
| Details | binding site for residue FMT A 511 |
| Chain | Residue |
| A | GLU350 |
| A | PHE353 |
| site_id | AD3 |
| Number of Residues | 10 |
| Details | binding site for residue GOL A 512 |
| Chain | Residue |
| A | MET1 |
| A | GLU105 |
| A | TYR106 |
| A | GLY220 |
| A | THR224 |
| A | SER254 |
| A | ARG255 |
| A | ALA258 |
| A | HOH753 |
| A | HOH902 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 513 |
| Chain | Residue |
| A | HOH684 |
| A | HOH903 |
| A | HOH1153 |
| A | HOH1159 |
| A | HOH1187 |
| A | HOH1342 |
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 |
