5JQ2
Crystal structure of the Ru(bpy)2PhenA functionalized P450 BM3 L407C heme domain mutant in complex 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 | 24 |
| 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 | HOH611 |
| A | LEU75 |
| A | HOH638 |
| A | HOH661 |
| A | HOH696 |
| A | HOH697 |
| A | HOH713 |
| A | LEU86 |
| A | PHE87 |
| A | TRP96 |
| A | ILE153 |
| A | ALA264 |
| A | GLY265 |
| A | THR268 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue 140 A 502 |
| Chain | Residue |
| A | LEU29 |
| A | TYR51 |
| A | SER72 |
| A | GLN73 |
| A | ALA74 |
| A | ALA82 |
| A | LEU188 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | binding site for residue RU8 A 503 |
| Chain | Residue |
| A | LYS309 |
| A | LYS312 |
| A | GLY315 |
| A | MET316 |
| A | LEU318 |
| A | ASN319 |
| A | PHE379 |
| A | CYS407 |
| B | ALA197 |
| B | TYR198 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | binding site for residue HEM B 501 |
| Chain | Residue |
| B | LYS69 |
| B | LEU75 |
| B | LEU86 |
| B | PHE87 |
| B | TRP96 |
| B | ALA264 |
| B | GLY265 |
| B | THR268 |
| B | THR269 |
| B | PHE331 |
| B | PRO392 |
| B | PHE393 |
| B | GLY394 |
| B | ARG398 |
| B | CYS400 |
| B | ILE401 |
| B | HOH604 |
| B | HOH624 |
| B | HOH647 |
| B | HOH667 |
| B | HOH722 |
| B | HOH736 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | binding site for residue 140 B 502 |
| Chain | Residue |
| B | LEU20 |
| B | PRO25 |
| B | PHE42 |
| B | ARG47 |
| B | TYR51 |
| B | ALA82 |
| B | LEU188 |
| B | HOH724 |
| B | HOH771 |
| B | HOH788 |
| site_id | AC6 |
| Number of Residues | 19 |
| Details | binding site for Di-peptide RU8 B 503 and CYS B 407 |
| Chain | Residue |
| B | ASN101 |
| B | PRO243 |
| B | LYS309 |
| B | LYS312 |
| B | GLY315 |
| B | MET316 |
| B | LEU318 |
| B | ASN319 |
| B | PHE379 |
| B | PRO382 |
| B | GLN403 |
| B | GLN404 |
| B | PHE405 |
| B | ALA406 |
| B | HIS408 |
| B | GLU409 |
| B | ALA410 |
| B | THR411 |
| B | HOH692 |
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 |
