Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0047040 | molecular_function | pteridine reductase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0047040 | molecular_function | pteridine reductase activity |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0047040 | molecular_function | pteridine reductase activity |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0047040 | molecular_function | pteridine reductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 32 |
| Details | binding site for residue NAP A 301 |
| Chain | Residue |
| A | LYS13 |
| A | LEU63 |
| A | THR64 |
| A | ASN93 |
| A | ALA94 |
| A | SER95 |
| A | THR126 |
| A | LEU159 |
| A | CYS160 |
| A | TYR174 |
| A | LYS178 |
| A | ARG14 |
| A | PRO204 |
| A | GLY205 |
| A | VAL206 |
| A | SER207 |
| A | LEU208 |
| A | EUH302 |
| A | HOH421 |
| A | HOH426 |
| A | HOH431 |
| A | HOH441 |
| A | ILE15 |
| A | HOH463 |
| A | HOH482 |
| A | HOH505 |
| A | TYR34 |
| A | HIS35 |
| A | ASN36 |
| A | SER37 |
| A | ALA61 |
| A | ASP62 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue EUH A 302 |
| Chain | Residue |
| A | SER95 |
| A | PHE97 |
| A | TYR174 |
| A | LEU209 |
| A | PRO210 |
| A | MET213 |
| A | TRP221 |
| A | NAP301 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 303 |
| Chain | Residue |
| A | ARG230 |
| A | GLU231 |
| A | HOH438 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue ACT A 304 |
| Chain | Residue |
| A | PHE243 |
| A | SER246 |
| A | HOH439 |
| A | HOH492 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue DMS A 305 |
| Chain | Residue |
| A | ASP161 |
| A | MET163 |
| A | PRO167 |
| A | CYS168 |
| A | TYR174 |
| A | ASN175 |
| site_id | AC6 |
| Number of Residues | 33 |
| Details | binding site for residue NAP B 301 |
| Chain | Residue |
| B | ARG14 |
| B | ILE15 |
| B | TYR34 |
| B | HIS35 |
| B | ASN36 |
| B | SER37 |
| B | ALA61 |
| B | ASP62 |
| B | LEU63 |
| B | THR64 |
| B | ASN93 |
| B | ALA94 |
| B | SER95 |
| B | THR126 |
| B | LEU159 |
| B | CYS160 |
| B | TYR174 |
| B | LYS178 |
| B | PRO204 |
| B | GLY205 |
| B | VAL206 |
| B | SER207 |
| B | LEU208 |
| B | EUH302 |
| B | HOH419 |
| B | HOH428 |
| B | HOH429 |
| B | HOH434 |
| B | HOH443 |
| B | HOH462 |
| B | HOH478 |
| B | HOH511 |
| B | HOH549 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | binding site for residue EUH B 302 |
| Chain | Residue |
| B | SER95 |
| B | PHE97 |
| B | ASP161 |
| B | TYR174 |
| B | LEU209 |
| B | PRO210 |
| B | TRP221 |
| B | NAP301 |
| B | DMS305 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue GOL B 303 |
| Chain | Residue |
| B | LEU208 |
| B | GLU231 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue ACT B 304 |
| Chain | Residue |
| B | HOH410 |
| B | HOH416 |
| C | VAL57 |
| C | VAL58 |
| B | TYR34 |
| B | VAL58 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue DMS B 305 |
| Chain | Residue |
| B | ASP161 |
| B | MET163 |
| B | PRO167 |
| B | CYS168 |
| B | TYR174 |
| B | ASN175 |
| B | EUH302 |
| site_id | AD2 |
| Number of Residues | 31 |
| Details | binding site for residue NAP C 301 |
| Chain | Residue |
| C | ARG14 |
| C | ILE15 |
| C | TYR34 |
| C | HIS35 |
| C | ASN36 |
| C | SER37 |
| C | ASP62 |
| C | LEU63 |
| C | THR64 |
| C | ASN93 |
| C | ALA94 |
| C | SER95 |
| C | THR126 |
| C | LEU159 |
| C | CYS160 |
| C | TYR174 |
| C | LYS178 |
| C | PRO204 |
| C | GLY205 |
| C | VAL206 |
| C | SER207 |
| C | LEU208 |
| C | EUH302 |
| C | HOH407 |
| C | HOH408 |
| C | HOH412 |
| C | HOH424 |
| C | HOH428 |
| C | HOH443 |
| C | HOH496 |
| C | HOH509 |
| site_id | AD3 |
| Number of Residues | 9 |
| Details | binding site for residue EUH C 302 |
| Chain | Residue |
| C | SER95 |
| C | PHE97 |
| C | ASP161 |
| C | TYR174 |
| C | LEU209 |
| C | PRO210 |
| C | MET213 |
| C | TRP221 |
| C | NAP301 |
| site_id | AD4 |
| Number of Residues | 11 |
| Details | binding site for residue GOL C 303 |
| Chain | Residue |
| B | ALA45 |
| B | ASP46 |
| B | ALA56 |
| B | VAL57 |
| B | VAL58 |
| B | HOH410 |
| B | HOH413 |
| C | TYR34 |
| C | VAL58 |
| C | GLN60 |
| C | HOH478 |
| site_id | AD5 |
| Number of Residues | 7 |
| Details | binding site for residue DMS C 304 |
| Chain | Residue |
| C | ASP161 |
| C | MET163 |
| C | PRO167 |
| C | CYS168 |
| C | TYR174 |
| C | ASN175 |
| C | HOH532 |
| site_id | AD6 |
| Number of Residues | 33 |
| Details | binding site for residue NAP D 301 |
| Chain | Residue |
| D | ARG14 |
| D | ILE15 |
| D | TYR34 |
| D | HIS35 |
| D | ASN36 |
| D | SER37 |
| D | ALA61 |
| D | ASP62 |
| D | LEU63 |
| D | THR64 |
| D | ASN93 |
| D | ALA94 |
| D | SER95 |
| D | THR126 |
| D | LEU159 |
| D | CYS160 |
| D | ASP161 |
| D | TYR174 |
| D | LYS178 |
| D | PRO204 |
| D | GLY205 |
| D | VAL206 |
| D | SER207 |
| D | LEU208 |
| D | EUH302 |
| D | HOH414 |
| D | HOH420 |
| D | HOH424 |
| D | HOH426 |
| D | HOH443 |
| D | HOH447 |
| D | HOH517 |
| D | HOH530 |
| site_id | AD7 |
| Number of Residues | 9 |
| Details | binding site for residue EUH D 302 |
| Chain | Residue |
| D | SER95 |
| D | PHE97 |
| D | ASP161 |
| D | TYR174 |
| D | LEU209 |
| D | PRO210 |
| D | MET213 |
| D | TRP221 |
| D | NAP301 |
| site_id | AD8 |
| Number of Residues | 6 |
| Details | binding site for residue DMS D 303 |
| Chain | Residue |
| D | ASP161 |
| D | MET163 |
| D | PRO167 |
| D | CYS168 |
| D | TYR174 |
| D | ASN175 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. DamvdqpcmaFslYNMGKHALvGLTqSAA |
| Chain | Residue | Details |
| A | ASP161-ALA189 | |
