3FSR
Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-295 of T. brockii ADH by C. beijerinckii ADH
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 353 |
| Chain | Residue |
| A | CYS37 |
| A | SER39 |
| A | HIS59 |
| A | ASP150 |
| A | EDO355 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ZN A 354 |
| Chain | Residue |
| A | EDO356 |
| A | HOH382 |
| C | TYR99 |
| A | GLY259 |
| A | GLY260 |
| A | HIS287 |
| A | THR289 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 355 |
| Chain | Residue |
| A | TRP110 |
| A | ASP150 |
| A | ZN353 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE EDO A 356 |
| Chain | Residue |
| A | ILE261 |
| A | THR289 |
| A | LYS291 |
| A | ZN354 |
| A | HOH382 |
| A | HOH456 |
| A | HOH476 |
| C | TYR99 |
| C | LYS291 |
| C | HOH862 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ZN B 353 |
| Chain | Residue |
| B | GLY259 |
| B | GLY260 |
| B | HIS287 |
| B | THR289 |
| D | TYR99 |
| D | HOH387 |
| D | HOH744 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN C 353 |
| Chain | Residue |
| C | CYS37 |
| C | SER39 |
| C | HIS59 |
| C | ASP150 |
| C | EDO354 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO C 354 |
| Chain | Residue |
| A | MET285 |
| C | ASP150 |
| C | TYR267 |
| C | ZN353 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN C 355 |
| Chain | Residue |
| A | TYR99 |
| A | HOH388 |
| C | GLY259 |
| C | GLY260 |
| C | HIS287 |
| C | THR289 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ZN D 353 |
| Chain | Residue |
| B | TYR99 |
| B | HOH627 |
| D | GLY259 |
| D | GLY260 |
| D | HIS287 |
| D | THR289 |
| D | HOH654 |
| site_id | BC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO D 354 |
| Chain | Residue |
| D | ASP150 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL D 355 |
| Chain | Residue |
| D | HIS222 |
| D | ILE223 |
| D | VAL224 |
| D | HOH658 |
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 |
