1ZO9
Crystal Structure Of The Wild Type Heme Domain Of P450BM-3 with N-palmitoylmethionine
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 471 |
| Chain | Residue |
| A | LYS69 |
| A | THR268 |
| A | THR269 |
| A | THR327 |
| A | PHE331 |
| A | PRO392 |
| A | PHE393 |
| A | GLY394 |
| A | ARG398 |
| A | ALA399 |
| A | CYS400 |
| A | LEU75 |
| A | ILE401 |
| A | HOH1486 |
| A | HOH1489 |
| A | HOH1491 |
| A | HOH1493 |
| A | HOH1503 |
| A | HOH1526 |
| A | HOH1535 |
| A | LEU86 |
| A | PHE87 |
| A | TRP96 |
| A | PHE107 |
| A | PHE261 |
| A | ALA264 |
| A | GLY265 |
| site_id | AC2 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE HEM B 471 |
| Chain | Residue |
| B | LYS69 |
| B | LEU75 |
| B | LEU86 |
| B | PHE87 |
| 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 | HOH1492 |
| B | HOH1494 |
| B | HOH1495 |
| B | HOH1516 |
| B | HOH1528 |
| B | HOH1551 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE EPM A 1470 |
| Chain | Residue |
| A | LEU29 |
| A | TYR51 |
| A | SER72 |
| A | GLN73 |
| A | ALA74 |
| A | VAL78 |
| A | ALA82 |
| A | LEU188 |
| A | THR260 |
| A | PRO329 |
| A | LEU437 |
| A | HOH1762 |
| A | HOH1927 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EPM B 1471 |
| Chain | Residue |
| B | LEU29 |
| B | TYR51 |
| B | SER72 |
| B | GLN73 |
| B | ALA74 |
| B | ALA82 |
| B | LEU188 |
| B | LEU437 |
| B | HOH1795 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MES B 1490 |
| Chain | Residue |
| B | ILE366 |
| B | TRP367 |
| B | ARG375 |
| B | ARG378 |
| B | ALA384 |
| B | ILE385 |
| B | PRO386 |
| B | HOH1975 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MES B 1491 |
| Chain | Residue |
| A | HOH1938 |
| B | HIS285 |
| B | HOH1570 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 1472 |
| Chain | Residue |
| A | LEU455 |
| A | GLY457 |
| A | HOH1829 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 1473 |
| Chain | Residue |
| A | GLU292 |
| A | ALA295 |
| A | ARG296 |
| A | HOH1787 |
| A | HOH1836 |
| A | HOH1986 |
| B | LYS59 |
| B | HOH1926 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 1474 |
| Chain | Residue |
| B | LYS312 |
| B | THR411 |
| B | HOH1539 |
| B | HOH1892 |
| B | VAL308 |
| B | LYS309 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 1475 |
| Chain | Residue |
| A | ASP34 |
| A | ARG362 |
| A | LYS364 |
| A | VAL371 |
| A | GLU372 |
| site_id | BC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 1476 |
| Chain | Residue |
| A | HOH1635 |
| A | HOH1720 |
| A | HOH1742 |
| A | HOH1743 |
| A | HOH1879 |
| B | LYS349 |
| B | GLY350 |
| B | HOH1972 |
| B | HOH2001 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 1477 |
| Chain | Residue |
| B | ARG79 |
| B | ASP84 |
| B | GLU252 |
| B | TYR256 |
| B | HOH1715 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 1478 |
| Chain | Residue |
| A | ILE220 |
| A | LEU238 |
| A | ASP251 |
| A | HOH1716 |
| A | HOH1797 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 1479 |
| Chain | Residue |
| B | LYS94 |
| B | GLU247 |
| B | LYS282 |
| B | HOH1718 |
| B | HOH1782 |
| B | HOH2021 |
| site_id | BC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 1480 |
| Chain | Residue |
| A | LYS391 |
| A | GLY394 |
| A | ASN395 |
| A | GLY396 |
| A | GLN403 |
| A | HOH1554 |
| A | HOH1964 |
| A | HOH2012 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 1481 |
| Chain | Residue |
| A | GLU143 |
| A | PRO170 |
| A | HOH1745 |
| A | HOH1915 |
| A | HOH1970 |
| site_id | BC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL A 1482 |
| Chain | Residue |
| A | ASP121 |
| A | ARG161 |
| site_id | BC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 1483 |
| Chain | Residue |
| A | ASP68 |
| A | THR91 |
| A | HIS92 |
| A | LYS336 |
| A | HOH1623 |
| A | HOH1734 |
| A | HOH1886 |
| site_id | CC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 1484 |
| Chain | Residue |
| A | GLN55 |
| A | LYS59 |
| A | HOH1610 |
| A | HOH1753 |
| B | GLN110 |
| site_id | CC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 1485 |
| Chain | Residue |
| A | GLU131 |
| A | ARG132 |
| A | HOH1992 |
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 | 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 |
