7OKZ
CRYSTAL STRUCTURE OF THE COFACTOR-DEVOID 1-H-3-HYDROXY-4- OXOQUINALDINE 2,4-DIOXYGENASE (HOD) CATALYTICALLY INACTIVE H251A VARIANT COMPLEXED WITH 2-METHYL- QUINOLIN-4(1H)-ONE UNDER HYPEROXIC CONDITIONS
This is a non-PDB format compatible entry.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| AAA | 0009056 | biological_process | catabolic process |
| AAA | 0016491 | molecular_function | oxidoreductase activity |
| AAA | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| AAA | 0050586 | molecular_function | 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase activity |
| AAA | 0051213 | molecular_function | dioxygenase activity |
| BBB | 0009056 | biological_process | catabolic process |
| BBB | 0016491 | molecular_function | oxidoreductase activity |
| BBB | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| BBB | 0050586 | molecular_function | 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase activity |
| BBB | 0051213 | molecular_function | dioxygenase activity |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 244 |
| Details | Domain: {"description":"AB hydrolase-1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"16187153","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Site: {"description":"Increases basicity of active site His","evidences":[{"source":"UniProtKB","id":"B1MFK2","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
