4HGJ
Crystal structure of P450 BM3 5F5 heme domain variant
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 | 25 |
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 | HOH609 |
A | LEU86 |
A | HOH611 |
A | HOH629 |
A | HOH651 |
A | HOH682 |
A | HOH760 |
A | HOH958 |
A | ALA87 |
A | TRP96 |
A | PHE107 |
A | PHE261 |
A | ALA264 |
A | GLY265 |
A | THR268 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 502 |
Chain | Residue |
A | LYS391 |
A | GLY394 |
A | ASN395 |
A | GLY396 |
A | GLN403 |
A | HOH742 |
A | HOH970 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 503 |
Chain | Residue |
A | ASP68 |
A | HIS92 |
A | LYS336 |
A | HOH726 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE MES A 504 |
Chain | Residue |
A | ILE366 |
A | TRP367 |
A | ARG375 |
A | ARG378 |
A | ALA384 |
A | ILE385 |
A | PRO386 |
A | HOH668 |
A | HOH924 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 505 |
Chain | Residue |
A | HIS100 |
A | GLY396 |
A | GLN397 |
A | ALA399 |
A | HOH682 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL B 501 |
Chain | Residue |
A | ASP121 |
B | GLN128 |
B | ARG132 |
site_id | AC7 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE HEM B 502 |
Chain | Residue |
B | LYS69 |
B | LEU86 |
B | ALA87 |
B | TRP96 |
B | PHE261 |
B | ALA264 |
B | GLY265 |
B | THR268 |
B | THR269 |
B | THR327 |
B | ALA328 |
B | PHE331 |
B | PRO392 |
B | PHE393 |
B | GLY394 |
B | ARG398 |
B | ALA399 |
B | CYS400 |
B | ILE401 |
B | PHE405 |
B | HOH610 |
B | HOH613 |
B | HOH615 |
B | HOH626 |
B | HOH646 |
B | HOH664 |
B | HOH669 |
B | HOH994 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL B 503 |
Chain | Residue |
B | ARG79 |
B | ASP84 |
B | HOH962 |
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 |