1ZOA
Crystal Structure Of A328V Mutant Of The Heme Domain Of P450Bm-3 With N-Palmitoylglycine
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 | VAL328 |
A | PHE331 |
A | PRO392 |
A | PHE393 |
A | GLY394 |
A | ARG398 |
A | ALA399 |
A | CYS400 |
A | LEU86 |
A | ILE401 |
A | HOH1471 |
A | HOH1474 |
A | HOH1476 |
A | HOH1478 |
A | HOH1488 |
A | HOH1510 |
A | PHE87 |
A | TRP96 |
A | PHE107 |
A | PHE261 |
A | ALA264 |
A | GLY265 |
A | THR268 |
site_id | AC2 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE HEM B 471 |
Chain | Residue |
B | LYS69 |
B | LEU86 |
B | PHE87 |
B | TRP96 |
B | PHE107 |
B | PHE261 |
B | ALA264 |
B | GLY265 |
B | THR268 |
B | THR269 |
B | LEU272 |
B | VAL328 |
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 | HOH1527 |
B | HOH1549 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE 140 A 1470 |
Chain | Residue |
A | LEU29 |
A | TYR51 |
A | SER72 |
A | GLN73 |
A | ALA74 |
A | ALA82 |
A | LEU188 |
A | ALA330 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE 140 B 1471 |
Chain | Residue |
B | LEU29 |
B | TYR51 |
B | SER72 |
B | GLN73 |
B | ALA74 |
B | ALA82 |
B | PHE87 |
B | LEU188 |
site_id | AC5 |
Number of Residues | 9 |
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 | MES1491 |
B | HOH1847 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MES B 1491 |
Chain | Residue |
B | THR365 |
B | ILE366 |
B | GLY368 |
B | PRO386 |
B | GOL1480 |
B | MES1490 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL B 1480 |
Chain | Residue |
A | HOH1737 |
A | HOH1825 |
B | ILE366 |
B | MES1491 |
B | HOH1524 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL B 1481 |
Chain | Residue |
B | ARG79 |
B | GLY83 |
B | TYR256 |
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 |