2WJ4
CRYSTAL STRUCTURE OF THE COFACTOR-DEVOID 1-H-3-HYDROXY-4- OXOQUINALDINE 2,4-DIOXYGENASE (HOD) FROM ARTHROBACTER NITROGUAJACOLICUS RU61A ANAEROBICALLY COMPLEXED WITH ITS NATURAL SUBSTRATE 1-H-3-HYDROXY-4-OXOQUINALDINE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| A | 0019335 | biological_process | methylquinoline catabolic process |
| 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 | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| B | 0019335 | biological_process | methylquinoline catabolic process |
| 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 | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| C | 0019335 | biological_process | methylquinoline catabolic process |
| 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 | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| D | 0019335 | biological_process | methylquinoline catabolic process |
| 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 | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 1276 |
| Chain | Residue |
| A | ASP158 |
| A | HOH2096 |
| C | ALA235 |
| C | TYR243 |
| C | K1276 |
| C | HOH2097 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 1277 |
| Chain | Residue |
| A | HOH2098 |
| D | ASP158 |
| D | VAL159 |
| A | ALA235 |
| A | K1279 |
| A | HOH2097 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL C 1275 |
| Chain | Residue |
| B | ALA235 |
| B | TYR243 |
| B | K1277 |
| B | HOH2088 |
| C | ASP158 |
| C | HOH2052 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 1278 |
| Chain | Residue |
| A | PRO146 |
| A | TRP149 |
| A | ARG150 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL D 1275 |
| Chain | Residue |
| D | GLY247 |
| D | GOL1276 |
| D | HOH2077 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL D 1276 |
| Chain | Residue |
| B | HIS164 |
| B | ASP165 |
| B | HOH2052 |
| D | LYS245 |
| D | LEU246 |
| D | GLY247 |
| D | GOL1275 |
| D | HOH2078 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 1276 |
| Chain | Residue |
| B | ASP158 |
| B | ASP162 |
| B | GLY163 |
| B | HOH2096 |
| D | SER232 |
| D | ALA235 |
| D | TYR243 |
| D | K1277 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE K C 1276 |
| Chain | Residue |
| A | GOL1276 |
| C | ALA235 |
| C | HIS238 |
| C | PHE241 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K B 1277 |
| Chain | Residue |
| B | ALA235 |
| B | HIS238 |
| B | PRO239 |
| B | PHE241 |
| C | GOL1275 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE K A 1279 |
| Chain | Residue |
| A | ALA235 |
| A | HIS238 |
| A | PRO239 |
| A | PHE241 |
| A | GOL1277 |
| A | HOH2086 |
| A | HOH2097 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K D 1277 |
| Chain | Residue |
| B | GOL1276 |
| D | ALA235 |
| D | HIS238 |
| D | PHE241 |
| D | HOH2066 |
| D | HOH2067 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE K A 1280 |
| Chain | Residue |
| A | ASP165 |
| A | SRT1283 |
| A | HOH2100 |
| C | HOH2098 |
| site_id | BC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE HQD A 1281 |
| Chain | Residue |
| A | TRP36 |
| A | HIS38 |
| A | HIS100 |
| A | SER101 |
| A | HIS102 |
| A | LEU143 |
| A | TRP160 |
| A | MET177 |
| A | TRP185 |
| A | SER188 |
| A | ILE192 |
| A | HIS251 |
| A | HOH2099 |
| site_id | BC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE HQD B 1278 |
| Chain | Residue |
| B | TRP36 |
| B | HIS38 |
| B | HIS100 |
| B | SER101 |
| B | HIS102 |
| B | LEU143 |
| B | TRP160 |
| B | MET177 |
| B | TRP185 |
| B | SER188 |
| B | ILE192 |
| B | HIS251 |
| B | HOH2097 |
| site_id | BC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE HQD C 1277 |
| Chain | Residue |
| C | TRP185 |
| C | SER188 |
| C | ILE192 |
| C | HIS251 |
| C | HOH2108 |
| C | TRP36 |
| C | HIS38 |
| C | HIS100 |
| C | SER101 |
| C | HIS102 |
| C | LEU143 |
| C | TRP160 |
| site_id | BC7 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE HQD D 1278 |
| Chain | Residue |
| D | TRP36 |
| D | HIS38 |
| D | HIS100 |
| D | SER101 |
| D | HIS102 |
| D | LEU143 |
| D | TRP160 |
| D | TRP185 |
| D | SER188 |
| D | ILE192 |
| D | HIS251 |
| D | HOH2079 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SRT A 1282 |
| Chain | Residue |
| A | LYS167 |
| A | ARG170 |
| A | HIS171 |
| C | ARG260 |
| C | VAL263 |
| site_id | BC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SRT B 1279 |
| Chain | Residue |
| B | LYS167 |
| B | ARG170 |
| B | HIS171 |
| D | ARG260 |
| D | VAL263 |
| site_id | CC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SRT C 1278 |
| Chain | Residue |
| B | ARG260 |
| B | VAL263 |
| C | LYS167 |
| C | ARG170 |
| C | HIS171 |
| site_id | CC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SRT D 1279 |
| Chain | Residue |
| A | ARG260 |
| A | VAL263 |
| D | LYS167 |
| D | ARG170 |
| D | HIS171 |
| site_id | CC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SRT A 1283 |
| Chain | Residue |
| A | HIS164 |
| A | ASP165 |
| A | K1280 |
| A | HOH2100 |
| C | LYS245 |
| C | LEU246 |
| C | GLY247 |
| site_id | CC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SRT B 1280 |
| Chain | Residue |
| B | LYS245 |
| B | HOH2098 |
| B | HOH2099 |
| C | HIS164 |
| C | ASP165 |
| C | GLU166 |
| site_id | CC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SRT A 1284 |
| Chain | Residue |
| A | LYS245 |
| A | LEU246 |
| A | GLY247 |
| A | HOH2101 |
| D | HIS164 |
| D | ASP165 |
| D | GLU166 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 488 |
| Details | Domain: {"description":"AB hydrolase-1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| 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 | 16 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Site: {"description":"Increases basicity of active site His","evidences":[{"source":"UniProtKB","id":"B1MFK2","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
