3G5F
Crystallographic analysis of cytochrome P450 cyp121
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 | 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 | 0046872 | molecular_function | metal ion binding |
| A | 0070025 | molecular_function | carbon monoxide binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 A 397 |
| Chain | Residue |
| A | ARG58 |
| A | HOH1118 |
| A | SER61 |
| A | MET62 |
| A | LYS63 |
| A | HIS343 |
| A | HOH611 |
| A | HOH616 |
| A | HOH710 |
| A | HOH1073 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 398 |
| Chain | Residue |
| A | SER12 |
| A | ARG17 |
| A | HOH406 |
| A | HOH947 |
| A | HOH988 |
| A | HOH1047 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 399 |
| Chain | Residue |
| A | VAL5 |
| A | LEU6 |
| A | LEU7 |
| A | ARG32 |
| A | ARG300 |
| A | HOH767 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 400 |
| Chain | Residue |
| A | ARG134 |
| A | PHE161 |
| A | ARG381 |
| A | ARG391 |
| A | HOH756 |
| A | HOH837 |
| A | HOH1116 |
| site_id | AC5 |
| 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 | PHE280 |
| A | LEU284 |
| A | ARG286 |
| A | ALA337 |
| A | PHE338 |
| A | GLY339 |
| A | HIS343 |
| A | CYS345 |
| A | PRO346 |
| A | HOH617 |
| A | HOH624 |
| A | HOH775 |
| A | HOH798 |
| A | HOH841 |
| A | HOH888 |
| A | HOH1000 |
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
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17028183","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19416919","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12435731","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17028183","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18818197","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19416919","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22890978","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23620594","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"axial binding residue"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Site: {"description":"Participates in a stacking interactions with the tyrosyl of cYY"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Site: {"description":"Important for the position of heme"} |
| Chain | Residue | Details |
