1JQB
Alcohol Dehydrogenase from Clostridium Beijerinckii: Crystal Structure of Mutant with Enhanced Thermal Stability
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008270 | molecular_function | zinc ion binding |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0050009 | molecular_function | isopropanol dehydrogenase (NADP+) activity |
B | 0008270 | molecular_function | zinc ion binding |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0050009 | molecular_function | isopropanol dehydrogenase (NADP+) activity |
C | 0008270 | molecular_function | zinc ion binding |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0046872 | molecular_function | metal ion binding |
C | 0050009 | molecular_function | isopropanol dehydrogenase (NADP+) activity |
D | 0008270 | molecular_function | zinc ion binding |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0046872 | molecular_function | metal ion binding |
D | 0050009 | molecular_function | isopropanol dehydrogenase (NADP+) activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ZN A 1353 |
Chain | Residue |
A | CYS1037 |
A | HIS1059 |
A | ASP1150 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 2353 |
Chain | Residue |
B | CYS2037 |
B | HIS2059 |
B | GLU2060 |
B | ASP2150 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ZN C 3353 |
Chain | Residue |
C | ASP3150 |
C | CYS3037 |
C | HIS3059 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN D 4353 |
Chain | Residue |
D | HOH112 |
D | CYS4037 |
D | HIS4059 |
D | ASP4150 |
Functional Information from PROSITE/UniProt
site_id | PS00059 |
Number of Residues | 15 |
Details | ADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEaVGEvvevGseV |
Chain | Residue | Details |
A | GLY1058-VAL1072 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 16 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"12381840","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20102159","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9836873","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 36 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"9836873","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1qlh |
Chain | Residue | Details |
A | SER1039 | |
A | HIS1042 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1qlh |
Chain | Residue | Details |
B | HIS2042 | |
B | SER2039 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1qlh |
Chain | Residue | Details |
C | HIS3042 | |
C | SER3039 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1qlh |
Chain | Residue | Details |
D | SER4039 | |
D | HIS4042 |