1ZO4
Crystal Structure Of A328S Mutant Of The Heme Domain Of P450BM-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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE HEM A 471 |
| Chain | Residue |
| A | LYS69 |
| A | LEU272 |
| A | THR327 |
| A | PHE331 |
| A | PRO392 |
| A | PHE393 |
| A | GLY394 |
| A | ARG398 |
| A | ALA399 |
| A | CYS400 |
| A | ILE401 |
| A | LEU86 |
| A | HOH1494 |
| A | HOH1499 |
| A | HOH1502 |
| A | HOH1504 |
| A | HOH1517 |
| A | HOH1796 |
| A | HOH1867 |
| A | PHE87 |
| A | TRP96 |
| A | PHE107 |
| A | ALA264 |
| A | GLY265 |
| A | THR268 |
| A | THR269 |
| site_id | AC2 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE HEM B 471 |
| Chain | Residue |
| B | LYS69 |
| B | LEU86 |
| B | PHE87 |
| B | TRP96 |
| B | PHE107 |
| 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 | ILE401 |
| B | ALA406 |
| B | HOH1493 |
| B | HOH1494 |
| B | HOH1496 |
| B | HOH1499 |
| B | HOH1500 |
| B | HOH1540 |
| B | HOH1895 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MES B 1490 |
| Chain | Residue |
| B | HIS285 |
| B | ARG375 |
| B | GLU377 |
| B | HOH1546 |
| B | HOH1871 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MES A 1491 |
| Chain | Residue |
| A | ILE366 |
| A | TRP367 |
| A | ARG375 |
| A | GLU377 |
| A | ARG378 |
| A | ALA384 |
| A | ILE385 |
| A | PRO386 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 1470 |
| Chain | Residue |
| A | GLN128 |
| A | ARG132 |
| B | ASP121 |
| B | ARG161 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 1471 |
| Chain | Residue |
| A | ASP338 |
| A | GLU348 |
| A | HOH1702 |
| A | HOH1810 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 1472 |
| Chain | Residue |
| A | TYR166 |
| A | ARG167 |
| A | HOH1550 |
| B | LYS129 |
| B | LEU133 |
| B | ASP168 |
| B | HOH1645 |
| B | HOH1718 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 1473 |
| Chain | Residue |
| A | ARG79 |
| A | HOH1790 |
| A | HOH1856 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL B 1474 |
| Chain | Residue |
| B | PHE390 |
| B | LYS391 |
| B | PRO392 |
| B | PHE393 |
| B | GLY394 |
| B | GLN403 |
| B | GOL1475 |
| B | HOH1559 |
| B | HOH1835 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 1475 |
| Chain | Residue |
| B | GOL1474 |
| B | LYS391 |
| B | GLY394 |
| B | ASN395 |
| B | GLY396 |
| B | GLN403 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 1477 |
| Chain | Residue |
| B | GLY83 |
| B | ASP84 |
| B | GLU252 |
| B | TYR256 |
| B | HOH1678 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 1478 |
| Chain | Residue |
| B | GLU247 |
| B | LYS282 |
| B | HOH1676 |
| B | HOH1879 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 1479 |
| Chain | Residue |
| A | ARG132 |
| B | ASP121 |
| B | VAL124 |
| B | HOH1668 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 1481 |
| Chain | Residue |
| A | HIS285 |
| A | LYS289 |
| A | GLU377 |
| A | HOH1690 |
| A | HOH1853 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 1482 |
| Chain | Residue |
| A | LYS289 |
| A | TYR313 |
| A | MET316 |
| A | GLU380 |
| A | HOH1731 |
| site_id | BC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 1483 |
| Chain | Residue |
| B | GLY240 |
| B | LYS241 |
| B | HOH1908 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 1484 |
| Chain | Residue |
| A | MET5 |
| A | LYS41 |
| A | ARG50 |
| A | HOH1597 |
| site_id | BC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 1485 |
| Chain | Residue |
| A | SER108 |
| A | GOL1487 |
| A | HOH1521 |
| A | HOH1528 |
| site_id | CC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 1486 |
| Chain | Residue |
| A | TRP130 |
| A | GLU131 |
| A | LEU133 |
| A | ASN134 |
| A | ALA448 |
| A | LYS449 |
| A | SER450 |
| A | HOH1586 |
| A | HOH1676 |
| site_id | CC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 1487 |
| Chain | Residue |
| A | HIS100 |
| A | GLY396 |
| A | GLN397 |
| A | GOL1485 |
| A | HOH1567 |
| A | HOH1658 |
| A | HOH1735 |
| site_id | CC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 1488 |
| Chain | Residue |
| B | VAL302 |
| B | PRO303 |
| B | SER304 |
| B | HOH1622 |
| B | HOH1868 |
| site_id | CC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 1489 |
| Chain | Residue |
| A | PRO25 |
| A | VAL26 |
| A | LEU29 |
| A | TYR51 |
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 | LEU52 | |
| B | LEU52 |
| 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 | 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 |
