4J14
Crystal Structure of Human Cytochrome P450 CYP46A1 with Posaconazole 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 | 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 | 0008203 | biological_process | cholesterol metabolic process |
A | 0008207 | biological_process | C21-steroid hormone metabolic process |
A | 0008395 | molecular_function | steroid hydroxylase activity |
A | 0016020 | cellular_component | membrane |
A | 0016125 | biological_process | sterol metabolic process |
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 | 0042995 | cellular_component | cell projection |
A | 0045202 | cellular_component | synapse |
A | 0046872 | molecular_function | metal ion binding |
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 | THR306 |
A | SER307 |
A | ALA367 |
A | THR370 |
A | PRO429 |
A | PHE430 |
A | SER431 |
A | ARG435 |
A | CYS437 |
A | ILE438 |
A | TYR109 |
A | PHE442 |
A | X2N602 |
A | HOH718 |
A | HOH730 |
A | LEU125 |
A | VAL126 |
A | TRP134 |
A | ARG138 |
A | PHE299 |
A | ALA302 |
A | GLY303 |
site_id | AC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE X2N A 602 |
Chain | Residue |
A | VAL79 |
A | PHE80 |
A | MET108 |
A | ALA111 |
A | PHE121 |
A | ARG226 |
A | THR298 |
A | ILE301 |
A | ALA302 |
A | THR306 |
A | SER338 |
A | ALA474 |
A | THR475 |
A | HEM601 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL A 603 |
Chain | Residue |
A | SER148 |
A | SER149 |
A | ALA273 |
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: axial binding residue => ECO:0000269|PubMed:18621681, ECO:0000269|PubMed:20667828, ECO:0000269|PubMed:23288837, ECO:0007744|PDB:2Q9F, ECO:0007744|PDB:2Q9G, ECO:0007744|PDB:3MDR, ECO:0007744|PDB:3MDT, ECO:0007744|PDB:3MDV, ECO:0007744|PDB:4ENH, ECO:0007744|PDB:4FIA, ECO:0007744|PDB:4J14 |
Chain | Residue | Details |
A | CYS437 |