Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0003858 | molecular_function | 3-hydroxybutyrate dehydrogenase activity |
A | 0006629 | biological_process | lipid metabolic process |
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 | 0006629 | biological_process | lipid metabolic process |
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 | 0006629 | biological_process | lipid metabolic process |
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 | 0006629 | biological_process | lipid metabolic process |
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 | |