3FTN
Q165E/S254K Double Mutant 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 354 |
| Chain | Residue |
| A | CYS37 |
| A | SER39 |
| A | HIS59 |
| A | ASP150 |
| A | ACT353 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACT A 353 |
| Chain | Residue |
| A | ZN354 |
| A | HOH366 |
| A | HOH393 |
| A | SER39 |
| A | TRP110 |
| A | ASP150 |
| A | LEU294 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 355 |
| Chain | Residue |
| A | GLY174 |
| A | ILE175 |
| A | GLY176 |
| A | GLY198 |
| A | SER199 |
| A | ARG200 |
| A | HOH469 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 356 |
| Chain | Residue |
| A | ASP163 |
| A | ILE261 |
| A | LYS291 |
| A | HOH394 |
| C | LYS291 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 358 |
| Chain | Residue |
| A | ARG301 |
| A | ARG304 |
| A | HOH521 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 359 |
| Chain | Residue |
| A | PHE327 |
| A | HOH622 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 360 |
| Chain | Residue |
| A | ARG304 |
| A | HOH550 |
| B | GLY167 |
| B | ASP237 |
| B | LYS257 |
| B | HOH530 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 355 |
| Chain | Residue |
| B | CYS37 |
| B | SER39 |
| B | HIS59 |
| B | ASP150 |
| B | ACT353 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACT B 353 |
| Chain | Residue |
| B | SER39 |
| B | TRP110 |
| B | ASP150 |
| B | LEU294 |
| B | ZN355 |
| B | HOH363 |
| B | HOH480 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 354 |
| Chain | Residue |
| B | GLU139 |
| B | PHE310 |
| B | LYS312 |
| B | HOH544 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 358 |
| Chain | Residue |
| B | ASP130 |
| B | ARG299 |
| B | GLU303 |
| B | HOH483 |
| B | HOH493 |
| B | HOH539 |
| C | SER93 |
| site_id | BC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL B 359 |
| Chain | Residue |
| B | ASP307 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 360 |
| Chain | Residue |
| B | GLY69 |
| B | SER70 |
| B | HOH495 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO C 356 |
| Chain | Residue |
| B | SER93 |
| B | GLN96 |
| C | ARG299 |
| C | GLU303 |
| C | HOH462 |
| site_id | BC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO C 359 |
| Chain | Residue |
| C | HOH514 |
| C | HOH585 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN C 353 |
| Chain | Residue |
| C | CYS37 |
| C | SER39 |
| C | HIS59 |
| C | ASP150 |
| C | ACT355 |
| site_id | BC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ACT C 354 |
| Chain | Residue |
| C | GLY271 |
| C | ASP272 |
| site_id | BC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACT C 355 |
| Chain | Residue |
| A | MET285 |
| C | SER39 |
| C | HIS59 |
| C | ASP150 |
| C | LEU294 |
| C | ZN353 |
| C | HOH465 |
| site_id | CC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO C 358 |
| Chain | Residue |
| C | HIS157 |
| C | GLU160 |
| C | EDO360 |
| C | HOH429 |
| C | HOH513 |
| site_id | CC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO C 360 |
| Chain | Residue |
| C | GLY98 |
| C | TYR99 |
| C | GLN101 |
| C | HIS157 |
| C | EDO358 |
| site_id | CC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN D 357 |
| Chain | Residue |
| D | CYS37 |
| D | SER39 |
| D | HIS59 |
| D | ASP150 |
| D | HOH395 |
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 |
