4ENH
Crystal Structure of Human Cytochrome P450 CYP46A1 with Fluvoxamine Bound
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006699 | biological_process | bile acid biosynthetic process |
| A | 0006707 | biological_process | cholesterol catabolic process |
| A | 0006805 | biological_process | xenobiotic metabolic process |
| A | 0007399 | biological_process | nervous system development |
| A | 0008202 | biological_process | steroid metabolic process |
| A | 0008203 | biological_process | cholesterol metabolic process |
| A | 0008207 | biological_process | C21-steroid hormone metabolic process |
| A | 0008395 | molecular_function | steroid hydroxylase activity |
| A | 0016125 | biological_process | sterol metabolic process |
| 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 | 0030425 | cellular_component | dendrite |
| A | 0033781 | molecular_function | cholesterol 24-hydroxylase activity |
| A | 0042448 | biological_process | progesterone metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050649 | molecular_function | testosterone 6-beta-hydroxylase activity |
| A | 0062184 | molecular_function | testosterone 16-beta-hydroxylase activity |
| A | 0098793 | cellular_component | presynapse |
| A | 0098794 | cellular_component | postsynapse |
| A | 1900271 | biological_process | regulation of long-term synaptic potentiation |
| A | 1903044 | biological_process | protein localization to membrane raft |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE HEM A 601 |
| Chain | Residue |
| A | LYS104 |
| A | SER307 |
| A | THR370 |
| A | PRO429 |
| A | PHE430 |
| A | SER431 |
| A | ARG435 |
| A | SER436 |
| A | CYS437 |
| A | ILE438 |
| A | GLY439 |
| A | TYR109 |
| A | PHE442 |
| A | FVX602 |
| A | HOH768 |
| A | HOH769 |
| A | LEU125 |
| A | TRP134 |
| A | ARG138 |
| A | PHE299 |
| A | ALA302 |
| A | GLY303 |
| A | THR306 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE FVX A 602 |
| Chain | Residue |
| A | PHE80 |
| A | PHE121 |
| A | ILE222 |
| A | ILE301 |
| A | ALA302 |
| A | THR306 |
| A | ALA367 |
| A | TRP368 |
| A | GLY369 |
| A | PHE371 |
| A | HEM601 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FSlGHRSCIG |
| Chain | Residue | Details |
| A | PHE430-GLY439 |
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":"18621681","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20667828","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23288837","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2Q9F","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2Q9G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3MDR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3MDT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3MDV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ENH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FIA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4J14","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
