6H1S
Structure of the BM3 heme domain in complex with fluconazole
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 | 13 |
Details | binding site for residue TPF A 501 |
Chain | Residue |
A | ALA74 |
A | HEM502 |
A | HOH723 |
A | HOH750 |
A | HOH798 |
A | LEU75 |
A | VAL78 |
A | PHE82 |
A | ALA264 |
A | GLU267 |
A | THR268 |
A | LEU437 |
A | THR438 |
site_id | AC2 |
Number of Residues | 23 |
Details | binding site for residue HEM A 502 |
Chain | Residue |
A | LYS69 |
A | LEU86 |
A | VAL87 |
A | TRP96 |
A | GLY265 |
A | THR268 |
A | THR269 |
A | PHE331 |
A | PRO392 |
A | PHE393 |
A | GLY394 |
A | ARG398 |
A | ALA399 |
A | CYS400 |
A | ILE401 |
A | GLY402 |
A | TPF501 |
A | HOH613 |
A | HOH676 |
A | HOH694 |
A | HOH723 |
A | HOH728 |
A | HOH738 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue PO4 A 503 |
Chain | Residue |
A | LYS391 |
A | ASN395 |
A | GLY396 |
A | HOH623 |
A | HOH629 |
A | HOH651 |
A | HOH745 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue PO4 A 504 |
Chain | Residue |
A | ARG223 |
A | GLU228 |
A | GLN229 |
A | SER230 |
A | ASP231 |
A | THR235 |
A | HOH705 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue PO4 A 505 |
Chain | Residue |
A | SER108 |
A | GLN109 |
A | LYS289 |
A | HOH633 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue PO4 A 506 |
Chain | Residue |
A | GLU137 |
A | HIS138 |
A | HOH780 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue EDO A 507 |
Chain | Residue |
A | THR22 |
A | ASP23 |
A | LYS24 |
A | HOH833 |
B | LYS349 |
site_id | AC8 |
Number of Residues | 7 |
Details | binding site for residue EDO A 508 |
Chain | Residue |
A | ASP68 |
A | TRP90 |
A | THR91 |
A | HIS92 |
A | TYR334 |
A | HOH602 |
A | HOH775 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue EDO A 509 |
Chain | Residue |
A | TRP130 |
A | GLU131 |
A | LEU133 |
A | ALA448 |
A | LYS449 |
A | SER450 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue EDO A 510 |
Chain | Residue |
A | VAL308 |
A | LYS309 |
A | HIS408 |
A | THR411 |
A | HOH742 |
site_id | AD2 |
Number of Residues | 15 |
Details | binding site for residue TPF B 501 |
Chain | Residue |
B | ALA74 |
B | LEU75 |
B | PHE82 |
B | VAL87 |
B | ILE263 |
B | ALA264 |
B | THR268 |
B | ALA328 |
B | PRO329 |
B | ALA330 |
B | LEU437 |
B | THR438 |
B | HEM502 |
B | HOH729 |
B | HOH775 |
site_id | AD3 |
Number of Residues | 24 |
Details | binding site for residue HEM B 502 |
Chain | Residue |
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 | TPF501 |
B | HOH607 |
B | HOH657 |
B | HOH697 |
B | HOH722 |
B | HOH727 |
B | LYS69 |
B | LEU86 |
B | VAL87 |
B | TRP96 |
site_id | AD4 |
Number of Residues | 4 |
Details | binding site for residue PO4 B 503 |
Chain | Residue |
B | GLU137 |
B | HIS138 |
B | HOH721 |
B | HOH742 |
site_id | AD5 |
Number of Residues | 2 |
Details | binding site for residue EDO B 504 |
Chain | Residue |
B | ILE366 |
B | ARG378 |
site_id | AD6 |
Number of Residues | 2 |
Details | binding site for residue EDO B 505 |
Chain | Residue |
B | ILE366 |
B | GLN397 |
site_id | AD7 |
Number of Residues | 4 |
Details | binding site for residue EDO B 506 |
Chain | Residue |
B | ASP23 |
B | GLU435 |
B | THR436 |
B | HOH609 |
site_id | AD8 |
Number of Residues | 3 |
Details | binding site for residue EDO B 507 |
Chain | Residue |
B | GLY315 |
B | ASN319 |
B | HOH622 |
site_id | AD9 |
Number of Residues | 5 |
Details | binding site for residue EDO B 508 |
Chain | Residue |
B | TRP130 |
B | LEU133 |
B | ALA448 |
B | LYS449 |
B | SER450 |
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 |