1CQX
Crystal structure of the flavohemoglobin from Alcaligenes eutrophus at 1.75 A resolution
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 | 4 |
| Details | BINDING SITE FOR RESIDUE NA A 490 |
| Chain | Residue |
| A | PRO96 |
| A | GLU100 |
| B | PRO96 |
| B | GLU100 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE HEM A 404 |
| Chain | Residue |
| A | ILE81 |
| A | HIS85 |
| A | LEU88 |
| A | TYR95 |
| A | VAL98 |
| A | TYR126 |
| A | LEU129 |
| A | ALA130 |
| A | DGG406 |
| A | HOH505 |
| A | HOH579 |
| A | TYR29 |
| A | VAL42 |
| A | PHE43 |
| A | ASN44 |
| A | ASN80 |
| site_id | AC3 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE FAD A 405 |
| Chain | Residue |
| A | ASN44 |
| A | ALA46 |
| A | HIS47 |
| A | TYR190 |
| A | ARG206 |
| A | GLN207 |
| A | TYR208 |
| A | SER209 |
| A | SER222 |
| A | VAL223 |
| A | LYS224 |
| A | GLU226 |
| A | GLY227 |
| A | GLN231 |
| A | PRO232 |
| A | GLY234 |
| A | TYR235 |
| A | VAL236 |
| A | SER237 |
| A | VAL395 |
| A | GLY397 |
| A | PRO398 |
| A | HOH518 |
| A | HOH519 |
| A | HOH536 |
| A | HOH539 |
| A | HOH623 |
| A | HOH624 |
| A | HOH649 |
| A | HOH650 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE DGG A 406 |
| Chain | Residue |
| A | TYR29 |
| A | PHE43 |
| A | ALA56 |
| A | ALA60 |
| A | LEU102 |
| A | LEU129 |
| A | ARG375 |
| A | TYR393 |
| A | HEM404 |
| A | HOH687 |
| A | HOH771 |
| site_id | AC5 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEM B 404 |
| Chain | Residue |
| B | TYR29 |
| B | VAL42 |
| B | PHE43 |
| B | ASN44 |
| B | ASN80 |
| B | LYS84 |
| B | HIS85 |
| B | LEU88 |
| B | VAL90 |
| B | TYR95 |
| B | VAL98 |
| B | TYR126 |
| B | ALA130 |
| B | DGG406 |
| B | HOH732 |
| B | HOH1504 |
| B | HOH1691 |
| B | HOH1705 |
| site_id | AC6 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE FAD B 405 |
| Chain | Residue |
| B | GLY397 |
| B | PRO398 |
| B | HOH1508 |
| B | HOH1521 |
| B | HOH1526 |
| B | HOH1542 |
| B | HOH1545 |
| B | HOH1553 |
| B | HOH1648 |
| B | ASN44 |
| B | ALA46 |
| B | HIS47 |
| B | TYR190 |
| B | ARG206 |
| B | GLN207 |
| B | TYR208 |
| B | SER209 |
| B | SER222 |
| B | VAL223 |
| B | LYS224 |
| B | GLU226 |
| B | GLY227 |
| B | GLN231 |
| B | PRO232 |
| B | GLY234 |
| B | TYR235 |
| B | VAL236 |
| B | SER237 |
| B | VAL395 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE DGG B 406 |
| Chain | Residue |
| B | PHE28 |
| B | TYR29 |
| B | ALA56 |
| B | ALA60 |
| B | ALA63 |
| B | ILE81 |
| B | VAL98 |
| B | ARG375 |
| B | TYR393 |
| B | HEM404 |
| B | HOH732 |
| B | HOH1681 |
| B | HOH1706 |
| B | HOH1816 |
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 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ndh |
| Chain | Residue | Details |
| A | TYR208 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ndh |
| Chain | Residue | Details |
| B | TYR208 |
