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 | 24 |
Details | BINDING SITE FOR RESIDUE NAD A 300 |
Chain | Residue |
A | GLY11 |
A | ASP63 |
A | LEU64 |
A | ASN90 |
A | GLY92 |
A | LEU113 |
A | ALA141 |
A | SER142 |
A | TYR155 |
A | LYS159 |
A | PRO185 |
A | THR13 |
A | GLY186 |
A | TRP187 |
A | VAL188 |
A | HOH1160 |
A | HOH1544 |
A | SER14 |
A | GLY15 |
A | ILE16 |
A | ASN34 |
A | GLY35 |
A | PHE36 |
A | ALA62 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 406 |
Chain | Residue |
A | ARG260 |
A | HOH1003 |
D | ARG260 |
D | HOH1004 |
D | HOH1005 |
D | HOH1006 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 401 |
Chain | Residue |
B | VAL147 |
B | ARG260 |
B | HOH1001 |
C | ARG260 |
C | HOH1002 |
site_id | AC4 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE NAD C 300 |
Chain | Residue |
C | GLY11 |
C | THR13 |
C | SER14 |
C | GLY15 |
C | ILE16 |
C | GLY35 |
C | PHE36 |
C | ALA62 |
C | ASP63 |
C | LEU64 |
C | ASN90 |
C | ALA91 |
C | LEU113 |
C | ILE140 |
C | ALA141 |
C | SER142 |
C | TYR155 |
C | LYS159 |
C | PRO185 |
C | GLY186 |
C | TRP187 |
C | VAL188 |
C | HOH1087 |
C | HOH1180 |
C | HOH1242 |
C | HOH1368 |
C | HOH1420 |
site_id | AC5 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE NAD D 300 |
Chain | Residue |
D | GLY11 |
D | THR13 |
D | SER14 |
D | GLY15 |
D | ILE16 |
D | ASN34 |
D | GLY35 |
D | PHE36 |
D | ALA62 |
D | ASP63 |
D | LEU64 |
D | SER65 |
D | ASN90 |
D | ALA141 |
D | SER142 |
D | TYR155 |
D | LYS159 |
D | PRO185 |
D | GLY186 |
D | TRP187 |
D | VAL188 |
D | HOH1124 |
D | HOH1466 |
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 | |