3OZV
The Crystal Structure of flavohemoglobin from R. eutrophus in complex with econazole
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 | 18 |
| Details | BINDING SITE FOR RESIDUE HEM B 404 |
| Chain | Residue |
| B | VAL42 |
| B | TYR95 |
| B | TYR126 |
| B | LEU129 |
| B | ALA130 |
| B | PRO398 |
| B | ASP399 |
| B | DGG406 |
| B | ECN411 |
| B | HOH429 |
| B | PHE43 |
| B | ASN44 |
| B | ILE81 |
| B | LYS84 |
| B | HIS85 |
| B | LEU88 |
| B | VAL90 |
| B | GLN94 |
| site_id | AC2 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE FAD B 405 |
| Chain | Residue |
| B | ASN44 |
| B | ALA46 |
| B | GLU49 |
| B | GLN50 |
| B | LYS84 |
| B | TYR190 |
| B | ARG206 |
| B | GLN207 |
| B | TYR208 |
| B | SER209 |
| B | SER222 |
| B | VAL223 |
| B | LYS224 |
| B | GLN231 |
| B | PRO232 |
| B | GLY234 |
| B | TYR235 |
| B | VAL236 |
| B | SER237 |
| B | VAL276 |
| B | THR279 |
| B | GLU394 |
| B | VAL395 |
| B | PHE396 |
| B | HOH409 |
| B | HOH415 |
| B | HOH423 |
| B | HOH452 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE DGG B 406 |
| Chain | Residue |
| B | ALA60 |
| B | ALA63 |
| B | GLU66 |
| B | VAL77 |
| B | ILE81 |
| B | TYR126 |
| B | LEU129 |
| B | GLU403 |
| B | HEM404 |
| B | ECN411 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE HEM A 404 |
| Chain | Residue |
| A | PHE43 |
| A | ASN44 |
| A | HIS47 |
| A | ILE81 |
| A | LYS84 |
| A | HIS85 |
| A | LEU88 |
| A | VAL90 |
| A | GLN94 |
| A | TYR95 |
| A | VAL98 |
| A | TYR126 |
| A | ALA130 |
| A | PRO398 |
| A | ECN411 |
| site_id | AC5 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE FAD A 405 |
| Chain | Residue |
| A | ASN44 |
| A | ALA46 |
| A | GLN48 |
| A | GLU49 |
| 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 |
| B | PRO15 |
| B | TYR62 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE DGG A 406 |
| Chain | Residue |
| A | LEU74 |
| A | VAL77 |
| A | ECN411 |
| A | ALA63 |
| A | ASN67 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 A 407 |
| Chain | Residue |
| A | MET310 |
| A | ARG311 |
| A | ASP312 |
| A | ARG313 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ECN B 411 |
| Chain | Residue |
| B | ILE24 |
| B | ILE25 |
| B | PHE28 |
| B | PHE43 |
| B | GLN53 |
| B | ALA56 |
| B | LEU57 |
| B | LEU102 |
| B | HEM404 |
| B | DGG406 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ECN A 411 |
| Chain | Residue |
| A | ILE24 |
| A | PHE43 |
| A | GLN53 |
| A | ALA56 |
| A | LEU57 |
| A | LEU102 |
| A | ILE106 |
| A | HEM404 |
| A | DGG406 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 274 |
| Details | Domain: {"description":"Globin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 220 |
| Details | Domain: {"description":"FAD-binding FR-type"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 508 |
| Details | Region: {"description":"Reductase"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Charge relay system"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"proximal binding residue"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 14 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Site: {"description":"Involved in heme-bound ligand stabilization and O-O bond activation"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | Site: {"description":"Influences the redox potential of the prosthetic heme and FAD groups"} |
| Chain | Residue | Details |
