4HGG
Crystal structure of P450 BM3 5F5R heme domain variant complexed with styrene
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE HEM A 501 |
| Chain | Residue |
| A | LYS69 |
| A | THR269 |
| A | PHE331 |
| A | PRO392 |
| A | PHE393 |
| A | GLY394 |
| A | ARG398 |
| A | ALA399 |
| A | CYS400 |
| A | ILE401 |
| A | GLY402 |
| A | LEU75 |
| A | ALA406 |
| A | SYN502 |
| A | HOH602 |
| A | HOH603 |
| A | HOH622 |
| A | HOH626 |
| A | HOH688 |
| A | HOH905 |
| A | LEU86 |
| A | ALA87 |
| A | TRP96 |
| A | PHE261 |
| A | ALA264 |
| A | GLY265 |
| A | THR268 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SYN A 502 |
| Chain | Residue |
| A | ALA264 |
| A | THR268 |
| A | HEM501 |
| A | HOH790 |
| A | HOH900 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MES A 503 |
| Chain | Residue |
| A | ILE366 |
| A | TRP367 |
| A | ARG375 |
| A | ARG378 |
| A | ALA384 |
| A | ILE385 |
| A | HOH663 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 504 |
| Chain | Residue |
| A | ASP68 |
| A | THR91 |
| A | HIS92 |
| A | TYR334 |
| A | LYS336 |
| A | HOH630 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 505 |
| Chain | Residue |
| A | GLN128 |
| A | GLU131 |
| A | ARG132 |
| A | HOH946 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 506 |
| Chain | Residue |
| A | HIS100 |
| A | GLY396 |
| A | GLN397 |
| A | ALA399 |
| A | ILE401 |
| A | HOH622 |
| B | ASN381 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL A 507 |
| Chain | Residue |
| A | ASP121 |
| A | ARG161 |
| site_id | AC8 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE HEM B 501 |
| Chain | Residue |
| B | LYS69 |
| B | LEU86 |
| B | ALA87 |
| B | TRP96 |
| B | PHE107 |
| B | PHE261 |
| B | ALA264 |
| B | GLY265 |
| B | THR268 |
| B | THR269 |
| B | THR327 |
| B | PHE331 |
| B | PRO392 |
| B | PHE393 |
| B | GLY394 |
| B | ARG398 |
| B | ALA399 |
| B | CYS400 |
| B | ILE401 |
| B | GLY402 |
| B | ALA406 |
| B | SYN502 |
| B | HOH605 |
| B | HOH607 |
| B | HOH609 |
| B | HOH617 |
| B | HOH626 |
| B | HOH799 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SYN B 502 |
| Chain | Residue |
| B | ALA264 |
| B | THR268 |
| B | HEM501 |
| B | HOH833 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 503 |
| Chain | Residue |
| B | ASP68 |
| B | THR91 |
| B | HIS92 |
| B | TYR334 |
| B | LYS336 |
| B | HOH866 |
| B | HOH883 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 504 |
| Chain | Residue |
| B | ALA399 |
| B | HOH607 |
| B | HIS100 |
| B | GLN397 |
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 | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15020590, ECO:0007744|PDB:1SMJ |
| Chain | Residue | Details |
| A | TYR51 | |
| B | TYR51 |
| Chain | Residue | Details |
| A | CYS400 | |
| B | CYS400 |
| 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 | THR268 | |
| B | THR268 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 699 |
| Chain | Residue | Details |
| A | THR268 | electrostatic stabiliser, steric role |
| A | PHE393 | electrostatic stabiliser, steric role |
| A | CYS400 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 699 |
| Chain | Residue | Details |
| B | THR268 | electrostatic stabiliser, steric role |
| B | PHE393 | electrostatic stabiliser, steric role |
| B | CYS400 | electrostatic stabiliser |
