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 | 3 |
| Details | BINDING SITE FOR RESIDUE ACT A 269 |
| Chain | Residue |
| A | LYS13 |
| A | ARG14 |
| A | ARG17 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT B 269 |
| Chain | Residue |
| A | GLN186 |
| A | GLY254 |
| A | ILE256 |
| B | LYS258 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT D 269 |
| Chain | Residue |
| C | ILE256 |
| D | LYS258 |
| C | GLN186 |
| C | GLY254 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT C 269 |
| Chain | Residue |
| C | LYS258 |
| D | GLN186 |
| D | GLY254 |
| D | ILE256 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE ACT C 270 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT A 270 |
| Chain | Residue |
| A | LYS258 |
| B | GLN186 |
| B | GLY254 |
| B | ILE256 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT A 271 |
| Chain | Residue |
| A | GLU215 |
| A | LYS218 |
| A | ARG222 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NA A 272 |
| Chain | Residue |
| A | LYS258 |
| A | SER264 |
| site_id | AC9 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE NAP A 273 |
| Chain | Residue |
| A | LYS13 |
| A | ARG14 |
| A | ILE15 |
| A | TYR34 |
| A | HIS35 |
| A | ASN36 |
| A | SER37 |
| A | ALA61 |
| A | ASP62 |
| A | LEU63 |
| A | THR64 |
| A | ASN93 |
| A | ALA94 |
| A | SER95 |
| A | THR126 |
| A | LEU159 |
| A | CYS160 |
| A | TYR174 |
| A | LYS178 |
| A | PRO204 |
| A | GLY205 |
| A | SER207 |
| A | LEU208 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE AX4 A 274 |
| Chain | Residue |
| A | ARG14 |
| A | SER95 |
| A | PHE97 |
| A | ASP161 |
| A | TYR174 |
| A | LEU208 |
| A | LEU209 |
| A | PRO210 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE DTT A 275 |
| Chain | Residue |
| A | CYS168 |
| A | PHE171 |
| A | TRP221 |
| site_id | BC3 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE NAP B 270 |
| 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 | SER207 |
| B | LEU208 |
| site_id | BC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE AX4 B 271 |
| Chain | Residue |
| B | ARG14 |
| B | SER95 |
| B | PHE97 |
| B | ASP161 |
| B | TYR174 |
| B | LEU208 |
| B | LEU209 |
| B | PRO210 |
| site_id | BC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE DTT B 272 |
| site_id | BC6 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE NAP C 271 |
| Chain | Residue |
| C | THR64 |
| C | ASN93 |
| C | ALA94 |
| C | SER95 |
| C | THR126 |
| C | LEU159 |
| C | CYS160 |
| C | TYR174 |
| C | LYS178 |
| C | PRO204 |
| C | GLY205 |
| C | SER207 |
| C | LEU208 |
| C | ARG14 |
| C | ILE15 |
| C | TYR34 |
| C | HIS35 |
| C | ASN36 |
| C | SER37 |
| C | ALA61 |
| C | ASP62 |
| C | LEU63 |
| site_id | BC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE AX4 C 272 |
| Chain | Residue |
| C | ARG14 |
| C | SER95 |
| C | PHE97 |
| C | ASP161 |
| C | TYR174 |
| C | LEU208 |
| C | LEU209 |
| C | PRO210 |
| site_id | BC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE DTT C 273 |
| Chain | Residue |
| C | CYS168 |
| C | TRP221 |
| site_id | BC9 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE NAP D 270 |
| Chain | Residue |
| D | LYS13 |
| D | ARG14 |
| D | ILE15 |
| D | HIS33 |
| 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 | TYR174 |
| D | LYS178 |
| D | PRO204 |
| D | GLY205 |
| D | SER207 |
| D | LEU208 |
| site_id | CC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE AX4 D 271 |
| Chain | Residue |
| D | ARG14 |
| D | SER95 |
| D | PHE97 |
| D | ASP161 |
| D | TYR174 |
| D | LEU208 |
| D | LEU209 |
| D | PRO210 |
| D | TRP221 |
| site_id | CC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE DTT D 272 |
| Chain | Residue |
| D | CYS168 |
| D | GLU217 |
| D | TRP221 |
| site_id | CC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE D1D A 276 |
| site_id | CC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE D1D B 273 |
| Chain | Residue |
| B | GLY205 |
| B | TRP221 |
| site_id | CC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE D1D C 274 |
| site_id | CC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE D1D D 273 |
| Chain | Residue |
| D | GLY205 |
| D | TRP221 |
| site_id | CC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL A 277 |
| Chain | Residue |
| A | ARG230 |
| A | GLU231 |
| site_id | CC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL B 274 |
| Chain | Residue |
| B | ASP161 |
| B | TYR174 |
| site_id | CC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 275 |
| Chain | Residue |
| B | ASP46 |
| C | TYR34 |
| C | GLN60 |
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 | |
| B | ASP161-ALA189 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | ASP165 | |
| site_id | CSA10 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | PHE171 | |
| C | LYS178 | |
| site_id | CSA11 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | PHE171 | |
| D | LYS178 | |
| site_id | CSA12 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | PHE171 | |
| B | LYS178 | |
| site_id | CSA13 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | TYR174 | |
| A | LYS178 | |
| site_id | CSA14 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | TYR174 | |
| C | LYS178 | |
| site_id | CSA15 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | TYR174 | |
| D | LYS178 | |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | ASP165 | |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | ASP165 | |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | ASP165 | |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | SER152 | |
| A | TYR174 | |
| A | LYS178 | |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | SER152 | |
| C | TYR174 | |
| C | LYS178 | |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | SER152 | |
| D | TYR174 | |
| D | LYS178 | |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | TYR174 | |
| B | LYS178 | |
| site_id | CSA9 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | PHE171 | |
| A | LYS178 | |
