2WJ3
CRYSTAL STRUCTURE OF THE COFACTOR-DEVOID 1-H-3-HYDROXY-4- OXOQUINALDINE 2,4-DIOXYGENASE (HOD) FROM ARTHROBACTER NITROGUAJACOLICUS RU61A
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0009056 | biological_process | catabolic process |
| A | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| A | 0050586 | molecular_function | 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase activity |
| A | 0051213 | molecular_function | dioxygenase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0009056 | biological_process | catabolic process |
| B | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| B | 0050586 | molecular_function | 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase activity |
| B | 0051213 | molecular_function | dioxygenase activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0009056 | biological_process | catabolic process |
| C | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| C | 0050586 | molecular_function | 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase activity |
| C | 0051213 | molecular_function | dioxygenase activity |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0009056 | biological_process | catabolic process |
| D | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| D | 0050586 | molecular_function | 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase activity |
| D | 0051213 | molecular_function | dioxygenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 1276 |
| Chain | Residue |
| A | ALA235 |
| A | TYR243 |
| D | ASP158 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL B 1276 |
| Chain | Residue |
| B | TRP160 |
| B | HIS251 |
| B | HOH2026 |
| B | SER101 |
| B | HIS102 |
| B | ASP126 |
| B | TRP127 |
| B | LEU128 |
| B | PHE136 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SRT A 1277 |
| Chain | Residue |
| A | LYS167 |
| A | ARG170 |
| A | HIS171 |
| C | ARG260 |
| C | VAL263 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SRT B 1277 |
| Chain | Residue |
| B | LYS167 |
| B | ARG170 |
| B | HIS171 |
| D | ARG260 |
| D | VAL263 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SRT C 1275 |
| Chain | Residue |
| B | ARG260 |
| B | VAL263 |
| C | LYS167 |
| C | ARG170 |
| C | HIS171 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SRT D 1275 |
| Chain | Residue |
| A | ARG260 |
| A | VAL263 |
| D | LYS167 |
| D | ARG170 |
| D | HIS171 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SRT C 1276 |
| Chain | Residue |
| A | HIS164 |
| A | ASP165 |
| C | LYS245 |
| C | LEU246 |
| C | GLY247 |
| C | HOH2086 |
| C | HOH2087 |
| C | HOH2088 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SRT B 1278 |
| Chain | Residue |
| B | LYS245 |
| B | LEU246 |
| B | GLY247 |
| B | HOH2069 |
| B | HOH2070 |
| B | HOH2071 |
| C | GLY163 |
| C | HIS164 |
| C | ASP165 |
| C | GLU166 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SRT D 1276 |
| Chain | Residue |
| B | HIS164 |
| B | ASP165 |
| B | HOH2040 |
| D | LYS245 |
| D | LEU246 |
| D | GLY247 |
| D | HOH2055 |
| D | HOH2056 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SRT A 1278 |
| Chain | Residue |
| A | LYS245 |
| A | LEU246 |
| A | GLY247 |
| A | HOH2064 |
| D | HIS164 |
| D | ASP165 |
| D | GLU166 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:16187153 |
| Chain | Residue | Details |
| A | HIS251 | |
| B | HIS251 | |
| C | HIS251 | |
| D | HIS251 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | TRP36 | |
| D | TRP36 | |
| D | HIS100 | |
| D | TRP160 | |
| A | HIS100 | |
| A | TRP160 | |
| B | TRP36 | |
| B | HIS100 | |
| B | TRP160 | |
| C | TRP36 | |
| C | HIS100 | |
| C | TRP160 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | SITE: Increases basicity of active site His => ECO:0000250|UniProtKB:B1MFK2 |
| Chain | Residue | Details |
| A | ASP126 | |
| B | ASP126 | |
| C | ASP126 | |
| D | ASP126 |
