Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004497 | molecular_function | monooxygenase activity |
A | 0005506 | molecular_function | iron ion binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0006707 | biological_process | cholesterol catabolic process |
A | 0008395 | molecular_function | steroid hydroxylase activity |
A | 0009975 | molecular_function | cyclase activity |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
A | 0016717 | molecular_function | oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water |
A | 0020037 | molecular_function | heme binding |
A | 0036199 | molecular_function | cholest-4-en-3-one 26-monooxygenase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0070025 | molecular_function | carbon monoxide binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 817 |
Chain | Residue |
A | LYS211 |
A | PRO330 |
A | ASN331 |
A | PRO332 |
A | THR333 |
A | SER334 |
A | HOH1215 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 819 |
Chain | Residue |
A | HOH1203 |
A | HOH1217 |
A | SER12 |
A | HOH1080 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 820 |
Chain | Residue |
A | ARG58 |
A | SER61 |
A | MET62 |
A | LYS63 |
A | HIS343 |
A | HOH955 |
A | HOH1001 |
site_id | AC4 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE HEM A 462 |
Chain | Residue |
A | MET62 |
A | MET86 |
A | HIS146 |
A | PHE230 |
A | GLY234 |
A | SER237 |
A | PHE241 |
A | PHE280 |
A | LEU284 |
A | ARG286 |
A | ALA337 |
A | PHE338 |
A | GLY339 |
A | HIS343 |
A | CYS345 |
A | PRO346 |
A | HOH843 |
A | HOH890 |
A | HOH902 |
A | HOH912 |
A | HOH923 |
A | HOH1045 |
Functional Information from PROSITE/UniProt
site_id | PS00086 |
Number of Residues | 10 |
Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGrGQHFCPG |
Chain | Residue | Details |
A | PHE338-GLY347 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | THR77 | |
A | SER237 | |
A | LYS301 | |
A | GLN385 | |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: |
Chain | Residue | Details |
A | ASN85 | |
Chain | Residue | Details |
A | ARG286 | |
A | HIS343 | |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: axial binding residue |
Chain | Residue | Details |
A | CYS345 | |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | SITE: Participates in a stacking interactions with the tyrosyl of cYY |
Chain | Residue | Details |
A | PHE168 | |
A | TRP182 | |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | SITE: Important for the position of heme |
Chain | Residue | Details |
A | PRO346 | |