6K9S
Structure of the Carbonylruthenium Mesoporphyrin IX-Reconstituted CYP102A1 Haem Domain with N-Abietoyl-L-Tryptophan
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 RUR A 501 |
| Chain | Residue |
| A | LYS69 |
| A | THR269 |
| A | THR327 |
| A | PHE331 |
| A | PRO392 |
| A | PHE393 |
| A | GLY394 |
| A | ARG398 |
| A | ALA399 |
| A | CYS400 |
| A | ILE401 |
| A | LEU86 |
| A | GLY402 |
| A | ALA406 |
| A | CMO502 |
| A | HOH634 |
| A | HOH653 |
| A | HOH661 |
| A | HOH687 |
| A | HOH731 |
| A | HOH769 |
| A | PHE87 |
| A | TRP96 |
| A | PHE107 |
| A | PHE261 |
| A | ALA264 |
| A | GLY265 |
| A | THR268 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue CMO A 502 |
| Chain | Residue |
| A | PHE87 |
| A | ALA264 |
| A | RUR501 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 503 |
| Chain | Residue |
| A | VAL308 |
| A | LYS309 |
| A | LEU311 |
| A | GLY315 |
| A | THR411 |
| A | HOH603 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 504 |
| Chain | Residue |
| A | ARG79 |
| A | GLY83 |
| A | ASP84 |
| A | GLU252 |
| A | TYR256 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 505 |
| Chain | Residue |
| A | GLN128 |
| A | GLU131 |
| A | ARG132 |
| B | ASP121 |
| B | ARG161 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 506 |
| Chain | Residue |
| A | GLN55 |
| A | LYS59 |
| A | ILE366 |
| A | PRO386 |
| A | HOH760 |
| B | GLU292 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 507 |
| Chain | Residue |
| A | ARG66 |
| A | THR339 |
| A | VAL340 |
| B | GLN310 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 508 |
| Chain | Residue |
| A | TRP130 |
| A | LEU133 |
| A | ASN134 |
| A | GLU137 |
| A | ALA448 |
| A | SER450 |
| A | HOH608 |
| site_id | AC9 |
| Number of Residues | 14 |
| Details | binding site for residue WAA A 509 |
| Chain | Residue |
| A | LEU20 |
| A | PRO25 |
| A | VAL26 |
| A | LEU29 |
| A | ARG47 |
| A | TYR51 |
| A | SER72 |
| A | GLN73 |
| A | ALA74 |
| A | LEU188 |
| A | ALA328 |
| A | ALA330 |
| A | MET354 |
| A | LEU437 |
| site_id | AD1 |
| Number of Residues | 28 |
| Details | binding site for residue RUR B 501 |
| Chain | Residue |
| B | CMO502 |
| B | HOH650 |
| B | HOH668 |
| B | HOH681 |
| B | HOH705 |
| B | HOH738 |
| B | HOH805 |
| 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 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue CMO B 502 |
| Chain | Residue |
| B | PHE87 |
| B | ALA264 |
| B | RUR501 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 503 |
| Chain | Residue |
| B | VAL308 |
| B | LYS309 |
| B | LEU311 |
| B | GLY315 |
| B | THR411 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 504 |
| Chain | Residue |
| B | ARG79 |
| B | GLY83 |
| B | ASP84 |
| B | GLU252 |
| B | TYR256 |
| B | HOH638 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 505 |
| Chain | Residue |
| B | ASP68 |
| B | HIS92 |
| B | LYS336 |
| B | HOH648 |
| site_id | AD6 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 506 |
| Chain | Residue |
| B | PRO142 |
| B | GLU143 |
| B | THR146 |
| B | LYS440 |
| B | HOH607 |
| B | HOH656 |
| site_id | AD7 |
| Number of Residues | 3 |
| Details | binding site for residue GOL B 507 |
| Chain | Residue |
| A | PRO382 |
| A | PHE390 |
| A | HOH707 |
| site_id | AD8 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 508 |
| Chain | Residue |
| B | TRP130 |
| B | LEU133 |
| B | ASN134 |
| B | ASP136 |
| B | ALA448 |
| B | LYS449 |
| B | SER450 |
| B | HOH613 |
| site_id | AD9 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 509 |
| Chain | Residue |
| B | ILE366 |
| B | ARG378 |
| B | ALA384 |
| B | PRO386 |
| B | HOH726 |
| site_id | AE1 |
| Number of Residues | 13 |
| Details | binding site for residue WAA B 510 |
| Chain | Residue |
| B | LEU20 |
| B | VAL26 |
| B | LEU29 |
| B | ARG47 |
| B | TYR51 |
| B | SER72 |
| B | GLN73 |
| B | ALA74 |
| B | LEU188 |
| B | ALA328 |
| B | ALA330 |
| B | MET354 |
| B | LEU437 |
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 |
