1PED
BACTERIAL SECONDARY ALCOHOL DEHYDROGENASE (APO-FORM)
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 | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 352 |
| Chain | Residue |
| A | CYS37 |
| A | HIS59 |
| A | GLU60 |
| A | ASP150 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 352 |
| Chain | Residue |
| B | CYS37 |
| B | HIS59 |
| B | GLU60 |
| B | ASP150 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 352 |
| Chain | Residue |
| C | CYS37 |
| C | HIS59 |
| C | GLU60 |
| C | ASP150 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 352 |
| Chain | Residue |
| D | CYS37 |
| D | HIS59 |
| D | GLU60 |
| D | ASP150 |
| site_id | S1 |
| Number of Residues | 4 |
| Details | CATALYTIC SITE. |
| Chain | Residue |
| A | CYS37 |
| A | HIS59 |
| A | ASP150 |
| A | ZN352 |
| site_id | S2 |
| Number of Residues | 4 |
| Details | CATALYTIC SITE. |
| Chain | Residue |
| B | CYS37 |
| B | HIS59 |
| B | ASP150 |
| B | ZN352 |
| site_id | S3 |
| Number of Residues | 4 |
| Details | CATALYTIC SITE. |
| Chain | Residue |
| C | HIS59 |
| C | ASP150 |
| C | ZN352 |
| C | CYS37 |
| site_id | S4 |
| Number of Residues | 4 |
| Details | CATALYTIC SITE. |
| Chain | Residue |
| D | CYS37 |
| D | HIS59 |
| D | ASP150 |
| D | ZN352 |
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 | GLY58-VAL72 |
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 | HIS42 | |
| A | SER39 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qlh |
| Chain | Residue | Details |
| B | HIS42 | |
| B | SER39 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qlh |
| Chain | Residue | Details |
| C | HIS42 | |
| C | SER39 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qlh |
| Chain | Residue | Details |
| D | HIS42 | |
| D | SER39 |
