6H1O
Structure of the BM3 heme domain in complex with voriconazole
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 | 29 |
| Details | binding site for residue HEM A 501 |
| Chain | Residue |
| A | LYS69 |
| A | THR268 |
| A | THR269 |
| A | THR327 |
| A | PHE331 |
| A | PRO392 |
| A | PHE393 |
| A | GLY394 |
| A | ARG398 |
| A | ALA399 |
| A | CYS400 |
| A | LEU75 |
| A | ILE401 |
| A | GLY402 |
| A | ALA406 |
| A | VOR502 |
| A | GOL508 |
| A | HOH633 |
| A | HOH638 |
| A | HOH685 |
| A | HOH697 |
| A | HOH719 |
| A | LEU86 |
| A | VAL87 |
| A | TRP96 |
| A | PHE107 |
| A | PHE261 |
| A | ALA264 |
| A | GLY265 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue VOR A 502 |
| Chain | Residue |
| A | PHE82 |
| A | VAL87 |
| A | THR260 |
| A | ILE263 |
| A | ALA264 |
| A | GLU267 |
| A | THR268 |
| A | HEM501 |
| A | GOL508 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue PO4 A 503 |
| Chain | Residue |
| A | ILE366 |
| A | ARG378 |
| A | ALA384 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue PO4 A 504 |
| Chain | Residue |
| A | VAL281 |
| A | LYS282 |
| A | ASP425 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue PO4 A 505 |
| Chain | Residue |
| A | GLU137 |
| A | HIS138 |
| A | HOH720 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | binding site for residue GOL A 506 |
| Chain | Residue |
| A | LYS97 |
| A | HIS100 |
| A | ASN101 |
| A | HOH630 |
| A | HOH659 |
| B | ILE366 |
| B | ARG378 |
| B | ALA384 |
| B | ILE385 |
| B | PRO386 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | binding site for residue GOL A 507 |
| Chain | Residue |
| A | ARG132 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 508 |
| Chain | Residue |
| A | LEU75 |
| A | ALA330 |
| A | HEM501 |
| A | VOR502 |
| A | HOH619 |
| A | HOH685 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 509 |
| Chain | Residue |
| A | PHE81 |
| A | ASN213 |
| A | ILE259 |
| site_id | AD1 |
| Number of Residues | 27 |
| Details | binding site for residue HEM B 501 |
| Chain | Residue |
| B | LYS69 |
| B | LEU75 |
| B | LEU86 |
| B | VAL87 |
| B | TRP96 |
| 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 | VOR502 |
| B | HOH623 |
| B | HOH647 |
| B | HOH689 |
| B | HOH722 |
| B | HOH785 |
| B | HOH876 |
| site_id | AD2 |
| Number of Residues | 12 |
| Details | binding site for residue VOR B 502 |
| Chain | Residue |
| B | ALA264 |
| B | GLU267 |
| B | THR268 |
| B | LEU437 |
| B | HEM501 |
| B | HOH755 |
| B | HOH824 |
| B | LEU75 |
| B | PHE82 |
| B | VAL87 |
| B | LEU181 |
| B | ILE263 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue PO4 B 503 |
| Chain | Residue |
| B | ASP80 |
| B | PHE81 |
| B | PHE205 |
| B | ILE209 |
| B | HOH802 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue PO4 B 504 |
| Chain | Residue |
| A | GLU4 |
| B | GLU247 |
| B | THR427 |
| B | ASN428 |
| B | HOH709 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 505 |
| Chain | Residue |
| B | VAL281 |
| B | ASP425 |
| B | ASN428 |
| B | HOH615 |
| B | HOH817 |
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 |
