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 | 0046872 | molecular_function | metal ion binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0003858 | molecular_function | 3-hydroxybutyrate dehydrogenase activity |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0046872 | molecular_function | metal ion binding |
C | 0000166 | molecular_function | nucleotide binding |
C | 0003858 | molecular_function | 3-hydroxybutyrate dehydrogenase activity |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0046872 | molecular_function | metal ion binding |
D | 0000166 | molecular_function | nucleotide binding |
D | 0003858 | molecular_function | 3-hydroxybutyrate dehydrogenase activity |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 31 |
Details | BINDING SITE FOR RESIDUE NAD A 300 |
Chain | Residue |
A | GLY11 |
A | ASP63 |
A | LEU64 |
A | ASN90 |
A | GLY92 |
A | LEU113 |
A | ILE140 |
A | ALA141 |
A | SER142 |
A | TYR155 |
A | LYS159 |
A | THR13 |
A | PRO185 |
A | GLY186 |
A | VAL188 |
A | SER190 |
A | PRO191 |
A | LEU192 |
A | VAL193 |
A | 3HL301 |
A | HOH1087 |
A | HOH1097 |
A | SER14 |
A | HOH1229 |
A | HOH1255 |
A | GLY15 |
A | ILE16 |
A | ASN34 |
A | GLY35 |
A | PHE36 |
A | ALA62 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE 3HL A 301 |
Chain | Residue |
A | GLN94 |
A | SER142 |
A | HIS144 |
A | LYS152 |
A | TYR155 |
A | LEU192 |
A | GLN196 |
A | NAD300 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 406 |
Chain | Residue |
A | ARG260 |
A | HOH1167 |
D | ARG260 |
D | HOH1018 |
D | HOH1318 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 401 |
Chain | Residue |
B | ARG260 |
B | HOH1013 |
B | HOH1135 |
C | ARG260 |
C | HOH1102 |
C | HOH1367 |
site_id | AC5 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE NAD C 300 |
Chain | Residue |
C | GLY11 |
C | THR13 |
C | SER14 |
C | GLY15 |
C | ILE16 |
C | ASN34 |
C | GLY35 |
C | PHE36 |
C | ALA62 |
C | ASP63 |
C | LEU64 |
C | ASN90 |
C | GLY92 |
C | LEU113 |
C | ILE140 |
C | ALA141 |
C | SER142 |
C | TYR155 |
C | LYS159 |
C | PRO185 |
C | GLY186 |
C | TRP187 |
C | VAL188 |
C | SER190 |
C | PRO191 |
C | LEU192 |
C | VAL193 |
C | HOH1011 |
site_id | AC6 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE NAD D 300 |
Chain | Residue |
D | GLY186 |
D | TRP187 |
D | VAL188 |
D | SER190 |
D | LEU192 |
D | VAL193 |
D | HOH1083 |
D | HOH1176 |
D | GLY11 |
D | THR13 |
D | SER14 |
D | GLY15 |
D | ILE16 |
D | ASN34 |
D | GLY35 |
D | PHE36 |
D | ALA62 |
D | ASP63 |
D | LEU64 |
D | ASN90 |
D | ALA91 |
D | GLY92 |
D | LEU113 |
D | ILE140 |
D | ALA141 |
D | SER142 |
D | TYR155 |
D | LYS159 |
D | PRO185 |
Functional Information from PROSITE/UniProt
site_id | PS00061 |
Number of Residues | 29 |
Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SahglvasanKsaYVAAKHGVvGFTkVTA |
Chain | Residue | Details |
A | SER142-ALA170 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
A | SER142 | |
A | TYR155 | |
A | LYS159 | |
site_id | CSA10 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
B | LYS152 | |
B | LYS159 | |
site_id | CSA11 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
C | LYS152 | |
C | LYS159 | |
site_id | CSA12 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
D | LYS152 | |
D | LYS159 | |
site_id | CSA13 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
A | TYR155 | |
A | LYS159 | |
site_id | CSA14 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
B | TYR155 | |
B | LYS159 | |
site_id | CSA15 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
C | TYR155 | |
C | LYS159 | |
site_id | CSA16 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
D | TYR155 | |
D | LYS159 | |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
B | SER142 | |
B | TYR155 | |
B | LYS159 | |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
C | SER142 | |
C | TYR155 | |
C | LYS159 | |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
D | SER142 | |
D | TYR155 | |
D | LYS159 | |
site_id | CSA5 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
A | TYR155 | |
A | SER142 | |
A | ASN114 | |
A | LYS159 | |
site_id | CSA6 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
B | TYR155 | |
B | SER142 | |
B | ASN114 | |
B | LYS159 | |
site_id | CSA7 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
C | TYR155 | |
C | SER142 | |
C | ASN114 | |
C | LYS159 | |
site_id | CSA8 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
D | TYR155 | |
D | SER142 | |
D | ASN114 | |
D | LYS159 | |
site_id | CSA9 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
A | LYS152 | |
A | LYS159 | |