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 | 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 | 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 | 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 |