Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003858 | molecular_function | 3-hydroxybutyrate dehydrogenase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0032787 | biological_process | monocarboxylic acid metabolic process |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003858 | molecular_function | 3-hydroxybutyrate dehydrogenase activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0032787 | biological_process | monocarboxylic acid metabolic process |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0003858 | molecular_function | 3-hydroxybutyrate dehydrogenase activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0032787 | biological_process | monocarboxylic acid metabolic process |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0003858 | molecular_function | 3-hydroxybutyrate dehydrogenase activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0032787 | biological_process | monocarboxylic acid metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAD B 300 |
| Chain | Residue |
| B | GLY12 |
| B | ASP60 |
| B | LEU61 |
| B | ASN87 |
| B | GLY89 |
| B | LYS106 |
| B | LEU110 |
| B | ALA138 |
| B | SER139 |
| B | TYR152 |
| B | LYS156 |
| B | THR14 |
| B | PRO182 |
| B | GLY183 |
| B | TRP184 |
| B | VAL185 |
| B | THR187 |
| B | PRO188 |
| B | LEU189 |
| B | VAL190 |
| B | HOH313 |
| B | HOH350 |
| B | SER15 |
| B | GLY16 |
| B | ILE17 |
| B | ASN35 |
| B | GLY36 |
| B | PHE37 |
| B | ALA59 |
| site_id | AC2 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAD C 300 |
| Chain | Residue |
| C | GLY12 |
| C | THR14 |
| C | SER15 |
| C | GLY16 |
| C | ILE17 |
| C | ASN35 |
| C | GLY36 |
| C | PHE37 |
| C | ALA59 |
| C | ASP60 |
| C | LEU61 |
| C | ASN87 |
| C | ALA88 |
| C | GLY89 |
| C | LEU110 |
| C | ILE137 |
| C | ALA138 |
| C | SER139 |
| C | TYR152 |
| C | LYS156 |
| C | PRO182 |
| C | GLY183 |
| C | TRP184 |
| C | VAL185 |
| C | THR187 |
| C | PRO188 |
| C | VAL190 |
| C | HOH330 |
| C | HOH350 |
| C | HOH355 |
| site_id | AC3 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAD D 300 |
| Chain | Residue |
| A | GLU102 |
| D | GLY12 |
| D | THR14 |
| D | SER15 |
| D | GLY16 |
| D | ILE17 |
| D | ASN35 |
| D | PHE37 |
| D | ALA59 |
| D | ASP60 |
| D | LEU61 |
| D | ASN87 |
| D | ALA88 |
| D | GLY89 |
| D | LEU110 |
| D | ILE137 |
| D | ALA138 |
| D | SER139 |
| D | TYR152 |
| D | LYS156 |
| D | PRO182 |
| D | GLY183 |
| D | TRP184 |
| D | VAL185 |
| D | THR187 |
| D | LEU189 |
| D | VAL190 |
| D | HOH311 |
| D | HOH350 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SvhglvgstgKaaYVAAKHGVvGLTkVVG |
| Chain | Residue | Details |
| A | SER139-GLY167 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | TYR152 | |
| A | LYS156 | |
| A | SER139 | |
| site_id | CSA10 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | LYS156 | |
| B | LYS149 | |
| site_id | CSA11 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | LYS156 | |
| C | LYS149 | |
| site_id | CSA12 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | LYS156 | |
| D | LYS149 | |
| site_id | CSA13 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | TYR152 | |
| A | LYS156 | |
| site_id | CSA14 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | TYR152 | |
| B | LYS156 | |
| site_id | CSA15 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | TYR152 | |
| C | LYS156 | |
| site_id | CSA16 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | TYR152 | |
| D | LYS156 | |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | TYR152 | |
| B | LYS156 | |
| B | SER139 | |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | TYR152 | |
| C | LYS156 | |
| C | SER139 | |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | TYR152 | |
| D | LYS156 | |
| D | SER139 | |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | ASN111 | |
| A | TYR152 | |
| A | LYS156 | |
| A | SER139 | |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | ASN111 | |
| B | TYR152 | |
| B | LYS156 | |
| B | SER139 | |
| site_id | CSA7 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | ASN111 | |
| C | TYR152 | |
| C | LYS156 | |
| C | SER139 | |
| site_id | CSA8 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | ASN111 | |
| D | TYR152 | |
| D | LYS156 | |
| D | SER139 | |
| site_id | CSA9 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | LYS156 | |
| A | LYS149 | |
