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 | 34 |
| Details | BINDING SITE FOR RESIDUE NAP A 269 |
| Chain | Residue |
| A | ARG14 |
| A | THR64 |
| A | ASN93 |
| A | ALA94 |
| A | SER95 |
| A | THR126 |
| A | LEU159 |
| A | CYS160 |
| A | ASP161 |
| A | TYR174 |
| A | LYS178 |
| A | ILE15 |
| A | PRO204 |
| A | GLY205 |
| A | VAL206 |
| A | SER207 |
| A | LEU208 |
| A | AX7271 |
| A | HOH293 |
| A | HOH296 |
| A | HOH315 |
| A | HOH320 |
| A | TYR34 |
| A | HOH329 |
| A | HOH372 |
| A | HOH384 |
| A | HOH417 |
| A | HOH471 |
| A | HIS35 |
| A | ASN36 |
| A | SER37 |
| A | ALA61 |
| A | ASP62 |
| A | LEU63 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE AX7 A 271 |
| Chain | Residue |
| A | PHE97 |
| A | ASP161 |
| A | TYR174 |
| A | NAP269 |
| A | HOH430 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT A 270 |
| Chain | Residue |
| A | LYS13 |
| A | ARG14 |
| A | ARG17 |
| A | HOH375 |
| A | HOH385 |
| A | HOH400 |
| site_id | AC4 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE NAP B 269 |
| Chain | Residue |
| B | ARG14 |
| B | ILE15 |
| B | HIS33 |
| 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 | ASP161 |
| B | TYR174 |
| B | LYS178 |
| B | PRO204 |
| B | GLY205 |
| B | VAL206 |
| B | SER207 |
| B | LEU208 |
| B | HOH490 |
| B | HOH494 |
| B | HOH498 |
| B | HOH517 |
| B | HOH522 |
| B | HOH544 |
| B | HOH556 |
| B | HOH573 |
| B | HOH584 |
| B | HOH622 |
| site_id | AC5 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAP C 269 |
| Chain | Residue |
| C | PRO204 |
| C | GLY205 |
| C | VAL206 |
| C | SER207 |
| C | LEU208 |
| C | AX7271 |
| C | HOH479 |
| C | HOH480 |
| C | HOH497 |
| C | HOH570 |
| C | HOH608 |
| C | HOH613 |
| C | HOH615 |
| C | HOH675 |
| C | ARG14 |
| C | ILE15 |
| C | TYR34 |
| C | HIS35 |
| C | ASN36 |
| C | SER37 |
| C | ALA61 |
| C | ASP62 |
| C | LEU63 |
| C | THR64 |
| C | ASN93 |
| C | ALA94 |
| C | SER95 |
| C | THR126 |
| C | LEU159 |
| C | CYS160 |
| C | ASP161 |
| C | TYR174 |
| C | LYS178 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE AX7 C 271 |
| Chain | Residue |
| C | PHE97 |
| C | ASP161 |
| C | TYR174 |
| C | NAP269 |
| C | HOH615 |
| C | HOH676 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT C 270 |
| Chain | Residue |
| B | TYR34 |
| B | VAL58 |
| B | HOH695 |
| C | VAL57 |
| C | VAL58 |
| C | HOH463 |
| site_id | AC8 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE NAP D 269 |
| Chain | Residue |
| 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 | VAL206 |
| D | SER207 |
| D | LEU208 |
| D | AX7270 |
| D | HOH387 |
| D | HOH395 |
| D | HOH423 |
| D | HOH453 |
| D | HOH514 |
| D | HOH520 |
| D | HOH527 |
| D | HOH536 |
| D | HOH553 |
| D | HOH563 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE AX7 D 270 |
| Chain | Residue |
| D | PHE97 |
| D | ASP161 |
| D | TYR174 |
| D | NAP269 |
| D | HOH514 |
| D | HOH546 |
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 | |
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 |
| B | PHE171 | |
| B | LYS178 | |
| site_id | CSA11 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | PHE171 | |
| C | LYS178 | |
| site_id | CSA12 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | PHE171 | |
| D | 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 |
| D | TYR174 | |
| D | LYS178 | |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | ASP165 | |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | ASP165 | |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | 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 | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | TYR174 | |
| B | LYS178 | |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | TYR174 | |
| C | LYS178 | |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | SER152 | |
| D | TYR174 | |
| D | LYS178 | |
| site_id | CSA9 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | PHE171 | |
| A | LYS178 | |
