7Y9L
Crystal structure of P450 BM3-2F from Bacillus megaterium in complex with 2-Hydroxy-5-Nitrobenzonitrile
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 | 6 |
| Details | binding site for residue 6VP A 1001 |
| Chain | Residue |
| A | PHE87 |
| A | ILE263 |
| A | ALA264 |
| A | GLU267 |
| A | THR438 |
| A | HEM1002 |
| site_id | AC2 |
| Number of Residues | 27 |
| Details | binding site for residue HEM A 1002 |
| Chain | Residue |
| A | TRP96 |
| A | PHE107 |
| A | PHE261 |
| A | ALA264 |
| A | GLY265 |
| A | THR268 |
| A | THR269 |
| A | THR327 |
| A | PHE331 |
| A | PRO392 |
| A | PHE393 |
| A | GLY394 |
| A | ARG398 |
| A | ALA399 |
| A | CYS400 |
| A | ILE401 |
| A | GLY402 |
| A | ALA406 |
| A | 6VP1001 |
| A | HOH1112 |
| A | HOH1124 |
| A | HOH1137 |
| A | HOH1160 |
| A | HOH1236 |
| A | LYS69 |
| A | LEU86 |
| A | PHE87 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue NI A 1003 |
| Chain | Residue |
| A | ASP231 |
| A | HIS236 |
| A | HOH1103 |
| A | HOH1131 |
| A | HOH1349 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue 6VP B 1001 |
| Chain | Residue |
| B | PHE87 |
| B | LEU181 |
| B | ILE263 |
| B | ALA264 |
| B | GLU267 |
| B | THR438 |
| B | HEM1002 |
| site_id | AC5 |
| Number of Residues | 27 |
| Details | binding site for residue HEM B 1002 |
| Chain | Residue |
| B | LYS69 |
| 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 | GLY402 |
| B | ALA406 |
| B | 6VP1001 |
| B | HOH1121 |
| B | HOH1139 |
| B | HOH1145 |
| B | HOH1168 |
| B | HOH1223 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue NI B 1003 |
| Chain | Residue |
| B | ASP231 |
| B | HIS236 |
| B | HOH1146 |
| B | HOH1237 |
| B | HOH1398 |
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 |
