2VOU
Structure of 2,6-dihydroxypyridine-3-hydroxylase from Arthrobacter nicotinovorans
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0018663 | molecular_function | 2,6-dihydroxypyridine 3-monooxygenase activity |
| A | 0019608 | biological_process | nicotine catabolic process |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0071949 | molecular_function | FAD binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0018663 | molecular_function | 2,6-dihydroxypyridine 3-monooxygenase activity |
| B | 0019608 | biological_process | nicotine catabolic process |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0071949 | molecular_function | FAD binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0018663 | molecular_function | 2,6-dihydroxypyridine 3-monooxygenase activity |
| C | 0019608 | biological_process | nicotine catabolic process |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0071949 | molecular_function | FAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE FAD A1395 |
| Chain | Residue |
| A | GLY12 |
| A | VAL49 |
| A | LYS118 |
| A | CYS119 |
| A | LEU120 |
| A | ALA148 |
| A | ASP149 |
| A | GLY150 |
| A | VAL154 |
| A | ARG173 |
| A | GLN222 |
| A | SER14 |
| A | GLY305 |
| A | ASP306 |
| A | ALA316 |
| A | ALA317 |
| A | GLY318 |
| A | GLY319 |
| A | ALA320 |
| A | GOL1396 |
| A | ACT1397 |
| A | HOH2065 |
| A | ILE15 |
| A | HOH2067 |
| A | HOH2187 |
| A | HOH2188 |
| A | HOH2189 |
| A | HOH2190 |
| A | HOH2191 |
| A | SER16 |
| A | TYR34 |
| A | GLU35 |
| A | ARG36 |
| A | LEU41 |
| A | ILE48 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A1396 |
| Chain | Residue |
| A | TYR206 |
| A | GLN222 |
| A | TYR224 |
| A | PRO313 |
| A | FAD1395 |
| A | HOH2192 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ACT A1397 |
| Chain | Residue |
| A | PRO311 |
| A | ARG312 |
| A | PRO313 |
| A | ALA316 |
| A | ALA317 |
| A | GLY318 |
| A | TYR357 |
| A | FAD1395 |
| A | HOH2159 |
| site_id | AC4 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE FAD B1389 |
| Chain | Residue |
| B | VAL11 |
| B | GLY12 |
| B | SER14 |
| B | ILE15 |
| B | SER16 |
| B | TYR34 |
| B | GLU35 |
| B | ARG36 |
| B | LEU41 |
| B | ILE48 |
| B | VAL49 |
| B | LYS118 |
| B | CYS119 |
| B | LEU120 |
| B | ALA148 |
| B | ASP149 |
| B | GLY150 |
| B | VAL154 |
| B | GLN222 |
| B | ASP306 |
| B | ALA316 |
| B | ALA317 |
| B | GLY318 |
| B | GLY319 |
| B | ALA320 |
| B | GOL1390 |
| B | ACT1391 |
| B | HOH2034 |
| B | HOH2125 |
| B | HOH2126 |
| B | HOH2127 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B1390 |
| Chain | Residue |
| B | TYR206 |
| B | GLN222 |
| B | TYR224 |
| B | PRO313 |
| B | FAD1389 |
| B | HOH2110 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ACT B1391 |
| Chain | Residue |
| B | ARG312 |
| B | PRO313 |
| B | ALA316 |
| B | ALA317 |
| B | GLY318 |
| B | TYR357 |
| B | FAD1389 |
| B | HOH2109 |
| site_id | AC7 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE FAD C1389 |
| Chain | Residue |
| C | SER16 |
| C | TYR34 |
| C | GLU35 |
| C | ARG36 |
| C | LEU41 |
| C | ILE48 |
| C | VAL49 |
| C | LYS118 |
| C | CYS119 |
| C | LEU120 |
| C | ASP149 |
| C | GLY150 |
| C | VAL154 |
| C | GLN222 |
| C | GLY305 |
| C | ASP306 |
| C | ALA316 |
| C | ALA317 |
| C | GLY318 |
| C | GLY319 |
| C | ALA320 |
| C | GOL1390 |
| C | ACT1391 |
| C | HOH2022 |
| C | HOH2066 |
| C | HOH2067 |
| C | HOH2068 |
| C | VAL11 |
| C | GLY12 |
| C | SER14 |
| C | ILE15 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL C1390 |
| Chain | Residue |
| C | TYR206 |
| C | GLN222 |
| C | TYR224 |
| C | PRO313 |
| C | ALA316 |
| C | FAD1389 |
| C | HOH2033 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ACT C1391 |
| Chain | Residue |
| C | PRO311 |
| C | ARG312 |
| C | PRO313 |
| C | ALA316 |
| C | ALA317 |
| C | GLY318 |
| C | TYR357 |
| C | FAD1389 |
| C | HOH2056 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 30 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18440023","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |






