6L1A
Crystal Structure of P450BM3 with N-enanthoyl-L-prolyl-L-phenylalanine
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 | 28 |
| Details | binding site for residue HEM A 501 |
| Chain | Residue |
| A | LYS69 |
| A | THR327 |
| A | PHE331 |
| A | PRO392 |
| A | PHE393 |
| A | GLY394 |
| A | ARG398 |
| A | ALA399 |
| A | CYS400 |
| A | ILE401 |
| A | GLY402 |
| A | LEU86 |
| A | PHE405 |
| A | ALA406 |
| A | DMS502 |
| A | HOH626 |
| A | HOH630 |
| A | HOH671 |
| A | HOH682 |
| A | HOH709 |
| A | HOH763 |
| A | PHE87 |
| A | TRP96 |
| A | ILE153 |
| A | ALA264 |
| A | THR268 |
| A | THR269 |
| A | LEU322 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue DMS A 502 |
| Chain | Residue |
| A | PHE87 |
| A | ALA264 |
| A | THR268 |
| A | HEM501 |
| A | OPF506 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 503 |
| Chain | Residue |
| A | LYS391 |
| A | GLY394 |
| A | ASN395 |
| A | GLY396 |
| A | GLN403 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 504 |
| Chain | Residue |
| A | ASP68 |
| A | HIS92 |
| A | LYS336 |
| A | HOH623 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 505 |
| Chain | Residue |
| A | TRP130 |
| A | LEU133 |
| A | ASN134 |
| A | ALA135 |
| A | ALA448 |
| A | LYS449 |
| A | SER450 |
| A | HOH601 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | binding site for residue OPF A 506 |
| Chain | Residue |
| A | LEU20 |
| A | LEU29 |
| A | ARG47 |
| A | TYR51 |
| A | SER72 |
| A | GLN73 |
| A | ALA74 |
| A | PHE87 |
| A | ALA328 |
| A | DMS502 |
| site_id | AC7 |
| Number of Residues | 30 |
| Details | binding site for residue HEM B 501 |
| Chain | Residue |
| B | LYS69 |
| B | LEU75 |
| B | LEU86 |
| B | PHE87 |
| B | TRP96 |
| B | ILE153 |
| B | ALA264 |
| B | THR268 |
| B | THR269 |
| B | LEU322 |
| B | THR327 |
| B | ALA328 |
| B | PHE331 |
| B | PRO392 |
| B | PHE393 |
| B | GLY394 |
| B | ARG398 |
| B | ALA399 |
| B | CYS400 |
| B | ILE401 |
| B | GLY402 |
| B | PHE405 |
| B | ALA406 |
| B | DMS502 |
| B | HOH618 |
| B | HOH627 |
| B | HOH638 |
| B | HOH683 |
| B | HOH698 |
| B | HOH741 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue DMS B 502 |
| Chain | Residue |
| B | PHE87 |
| B | ALA264 |
| B | THR268 |
| B | HEM501 |
| B | OPF504 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 503 |
| Chain | Residue |
| B | HOH642 |
| B | HOH751 |
| A | PRO196 |
| B | VAL297 |
| B | VAL299 |
| B | GLN307 |
| site_id | AD1 |
| Number of Residues | 14 |
| Details | binding site for residue OPF B 504 |
| Chain | Residue |
| B | LEU20 |
| B | VAL26 |
| B | LEU29 |
| B | ARG47 |
| B | TYR51 |
| B | SER72 |
| B | GLN73 |
| B | ALA74 |
| B | PHE87 |
| B | LEU188 |
| B | ALA330 |
| B | LEU437 |
| B | DMS502 |
| B | HOH667 |
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 |
| B | TYR51 | |
| A | TYR51 |
| Chain | Residue | Details |
| B | CYS400 | |
| A | 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 |
| B | THR268 | |
| A | 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 |
