3OZW
The Crystal Structure of flavohemoglobin from R. eutrophus in complex with ketoconazole
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005344 | molecular_function | oxygen carrier activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0008941 | molecular_function | nitric oxide dioxygenase NAD(P)H activity |
A | 0009636 | biological_process | response to toxic substance |
A | 0015671 | biological_process | oxygen transport |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0019825 | molecular_function | oxygen binding |
A | 0020037 | molecular_function | heme binding |
A | 0046210 | biological_process | nitric oxide catabolic process |
A | 0046872 | molecular_function | metal ion binding |
A | 0051409 | biological_process | response to nitrosative stress |
A | 0071500 | biological_process | cellular response to nitrosative stress |
A | 0071949 | molecular_function | FAD binding |
B | 0005344 | molecular_function | oxygen carrier activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0008941 | molecular_function | nitric oxide dioxygenase NAD(P)H activity |
B | 0009636 | biological_process | response to toxic substance |
B | 0015671 | biological_process | oxygen transport |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0019825 | molecular_function | oxygen binding |
B | 0020037 | molecular_function | heme binding |
B | 0046210 | biological_process | nitric oxide catabolic process |
B | 0046872 | molecular_function | metal ion binding |
B | 0051409 | biological_process | response to nitrosative stress |
B | 0071500 | biological_process | cellular response to nitrosative stress |
B | 0071949 | molecular_function | FAD binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE HEM A 404 |
Chain | Residue |
A | VAL42 |
A | TYR95 |
A | VAL98 |
A | TYR126 |
A | ALA130 |
A | PRO398 |
A | ASP399 |
A | KKK413 |
A | HOH485 |
A | PHE43 |
A | ASN44 |
A | ILE81 |
A | LYS84 |
A | HIS85 |
A | LEU88 |
A | VAL90 |
A | GLN94 |
site_id | AC2 |
Number of Residues | 31 |
Details | BINDING SITE FOR RESIDUE FAD A 405 |
Chain | Residue |
A | ASN44 |
A | ALA46 |
A | GLU49 |
A | GLN50 |
A | TYR190 |
A | ARG206 |
A | GLN207 |
A | TYR208 |
A | SER209 |
A | SER222 |
A | VAL223 |
A | LYS224 |
A | GLU226 |
A | GLN231 |
A | PRO232 |
A | GLY234 |
A | TYR235 |
A | VAL236 |
A | SER237 |
A | VAL276 |
A | THR279 |
A | VAL395 |
A | PHE396 |
A | GLY397 |
A | KKK413 |
A | HOH454 |
A | HOH455 |
A | HOH481 |
A | HOH484 |
B | PRO15 |
B | TYR62 |
site_id | AC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE KKK A 413 |
Chain | Residue |
A | TYR29 |
A | GLN50 |
A | GLN53 |
A | ALA56 |
A | LEU57 |
A | LEU102 |
A | PRO398 |
A | HEM404 |
A | FAD405 |
A | DGG416 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE DGG A 416 |
Chain | Residue |
A | ALA60 |
A | ALA63 |
A | TYR64 |
A | ASN67 |
A | LEU74 |
A | VAL77 |
A | TRP122 |
A | KKK413 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 A 406 |
Chain | Residue |
A | MET310 |
A | ARG311 |
A | ASP312 |
A | ARG313 |
site_id | AC6 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE FAD B 405 |
Chain | Residue |
B | HOH489 |
B | ASN44 |
B | ALA46 |
B | GLU49 |
B | GLN50 |
B | TYR190 |
B | ARG206 |
B | GLN207 |
B | TYR208 |
B | SER209 |
B | SER222 |
B | VAL223 |
B | LYS224 |
B | GLU226 |
B | GLN231 |
B | PRO232 |
B | GLY234 |
B | TYR235 |
B | VAL236 |
B | SER237 |
B | VAL276 |
B | THR279 |
B | VAL395 |
B | PHE396 |
B | HOH420 |
B | HOH422 |
B | HOH433 |
B | HOH467 |
B | HOH477 |
B | HOH485 |
site_id | AC7 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE HEM B 404 |
Chain | Residue |
B | VAL42 |
B | PHE43 |
B | ASN44 |
B | ILE81 |
B | LYS84 |
B | HIS85 |
B | LEU88 |
B | VAL90 |
B | GLN94 |
B | TYR95 |
B | TYR126 |
B | LEU129 |
B | ALA130 |
B | ASP399 |
B | KKK413 |
B | HOH469 |
B | HOH471 |
site_id | AC8 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE KKK B 413 |
Chain | Residue |
B | ILE25 |
B | PHE28 |
B | TYR29 |
B | HIS47 |
B | GLN52 |
B | GLN53 |
B | ALA56 |
B | LEU57 |
B | LEU102 |
B | GLY397 |
B | PRO398 |
B | HEM404 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Charge relay system |
Chain | Residue | Details |
A | TYR95 | |
A | GLU137 | |
B | TYR95 | |
B | GLU137 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: proximal binding residue |
Chain | Residue | Details |
A | HIS85 | |
B | HIS85 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | BINDING: |
Chain | Residue | Details |
A | TYR190 | |
A | ARG206 | |
A | VAL395 | |
B | TYR190 | |
B | ARG206 | |
B | VAL395 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | GLY275 | |
B | GLY275 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | SITE: Involved in heme-bound ligand stabilization and O-O bond activation |
Chain | Residue | Details |
A | TYR29 | |
B | TYR29 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | SITE: Influences the redox potential of the prosthetic heme and FAD groups |
Chain | Residue | Details |
A | LYS84 | |
A | GLU394 | |
B | LYS84 | |
B | GLU394 |