1BVY
COMPLEX OF THE HEME AND FMN-BINDING DOMAINS OF THE CYTOCHROME P450(BM-3)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| A | 0020037 | molecular_function | heme binding |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| B | 0020037 | molecular_function | heme binding |
| F | 0010181 | molecular_function | FMN binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE HEM A 1000 |
| Chain | Residue |
| A | LYS69 |
| A | PHE331 |
| A | PRO392 |
| A | PHE393 |
| A | GLY394 |
| A | ARG398 |
| A | ALA399 |
| A | CYS400 |
| A | GLY402 |
| A | EDO1003 |
| A | HOH1029 |
| A | LEU86 |
| A | HOH1042 |
| A | HOH1043 |
| A | HOH1067 |
| A | HOH1111 |
| A | HOH1147 |
| A | PHE87 |
| A | TRP96 |
| A | ALA264 |
| A | GLY265 |
| A | THR268 |
| A | THR269 |
| A | THR327 |
| site_id | AC2 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE FMN F 1002 |
| Chain | Residue |
| F | SER488 |
| F | ASN489 |
| F | MET490 |
| F | GLY491 |
| F | THR492 |
| F | ALA493 |
| F | ALA534 |
| F | SER535 |
| F | TYR536 |
| F | ASN537 |
| F | GLY538 |
| F | CYS569 |
| F | GLY570 |
| F | ASP571 |
| F | TRP574 |
| F | THR577 |
| F | TYR578 |
| F | GLN579 |
| F | HOH1007 |
| F | HOH1026 |
| F | HOH1034 |
| site_id | AC3 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE HEM B 1001 |
| Chain | Residue |
| B | LYS69 |
| B | LEU86 |
| B | PHE87 |
| B | TRP96 |
| B | ALA264 |
| B | GLY265 |
| B | THR268 |
| B | THR269 |
| B | LEU272 |
| B | THR327 |
| B | PHE331 |
| B | PRO392 |
| B | PHE393 |
| B | GLY394 |
| B | ARG398 |
| B | ALA399 |
| B | CYS400 |
| B | EDO1004 |
| B | HOH1021 |
| B | HOH1087 |
| B | HOH1089 |
| B | HOH1090 |
| B | HOH1091 |
| B | HOH1118 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 1003 |
| Chain | Residue |
| A | PHE87 |
| A | ALA264 |
| A | THR268 |
| A | ALA328 |
| A | HEM1000 |
| A | HOH1188 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 1004 |
| Chain | Residue |
| B | PHE87 |
| B | ALA264 |
| B | THR268 |
| B | ALA328 |
| B | HEM1001 |
| B | HOH1045 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 1005 |
| Chain | Residue |
| B | ILE39 |
| B | ARG50 |
| B | TYR345 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 1006 |
| Chain | Residue |
| A | PRO105 |
| A | SER108 |
| A | GLN110 |
| F | GLY495 |
| F | ASP499 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 1007 |
| Chain | Residue |
| B | TRP130 |
| B | LEU133 |
| B | ALA448 |
| B | HOH1048 |
| B | HOH1049 |
| B | HOH1179 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGnGQRACIG |
| Chain | Residue | Details |
| A | PHE393-GLY402 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10051560, ECO:0007744|PDB:1BVY |
| Chain | Residue | Details |
| F | ASN489 | |
| F | TYR536 | |
| F | GLY570 | |
| F | TYR578 |
| Chain | Residue | Details |
| A | ILE401 | |
| B | ILE401 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | SITE: Important for catalytic activity => ECO:0000305|PubMed:16403573, ECO:0000305|PubMed:7578081 |
| Chain | Residue | Details |
| A | THR269 | |
| B | THR269 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1akd |
| Chain | Residue | Details |
| A | THR268 | |
| A | GLU267 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1akd |
| Chain | Residue | Details |
| B | THR268 | |
| B | GLU267 |
| site_id | MCSA1 |
| Number of Residues | |
| Details | M-CSA 699 |
| Chain | Residue | Details |
| A | THR269 | electrostatic stabiliser, steric role |
| A | GLY394 | electrostatic stabiliser, steric role |
| A | ILE401 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 699 |
| Chain | Residue | Details |
| B | THR269 | electrostatic stabiliser, steric role |
| B | GLY394 | electrostatic stabiliser, steric role |
| B | ILE401 | electrostatic stabiliser |
