3WDS
Crystal structure of 3-quinuclidinone reductase from Agrobacterium tumefaciens
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0006633 | biological_process | fatty acid biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| A | 0048038 | molecular_function | quinone binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0006633 | biological_process | fatty acid biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| B | 0048038 | molecular_function | quinone binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0006633 | biological_process | fatty acid biosynthetic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| C | 0048038 | molecular_function | quinone binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0006633 | biological_process | fatty acid biosynthetic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| D | 0048038 | molecular_function | quinone binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAD A 301 |
| Chain | Residue |
| A | SER18 |
| A | ASN90 |
| A | ALA91 |
| A | GLY92 |
| A | THR141 |
| A | ALA142 |
| A | SER143 |
| A | TYR156 |
| A | LYS160 |
| A | PRO186 |
| A | GLY187 |
| A | LYS19 |
| A | VAL189 |
| A | THR191 |
| A | MET193 |
| A | ARG196 |
| A | HOH409 |
| A | HOH419 |
| A | HOH431 |
| A | HOH484 |
| A | HOH485 |
| A | HOH503 |
| A | GLY20 |
| A | HOH509 |
| A | ILE21 |
| A | ASP40 |
| A | LEU41 |
| A | VAL62 |
| A | ASP63 |
| A | VAL64 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ACY A 302 |
| Chain | Residue |
| A | ASN252 |
| A | VAL253 |
| A | THR254 |
| A | GLY255 |
| A | GLY256 |
| A | ARG258 |
| B | PHE245 |
| B | MET246 |
| B | THR247 |
| B | GLN249 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 303 |
| Chain | Residue |
| A | GLU61 |
| A | SER69 |
| A | HOH454 |
| site_id | AC4 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAD B 301 |
| Chain | Residue |
| B | GLY16 |
| B | SER18 |
| B | LYS19 |
| B | GLY20 |
| B | ILE21 |
| B | ASP40 |
| B | LEU41 |
| B | VAL62 |
| B | ASP63 |
| B | VAL64 |
| B | ASN90 |
| B | ALA91 |
| B | GLY92 |
| B | THR141 |
| B | ALA142 |
| B | SER143 |
| B | TYR156 |
| B | LYS160 |
| B | PRO186 |
| B | GLY187 |
| B | VAL189 |
| B | THR191 |
| B | MET193 |
| B | ARG196 |
| B | HOH410 |
| B | HOH433 |
| B | HOH489 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ACY B 302 |
| Chain | Residue |
| A | PHE245 |
| A | MET246 |
| A | THR247 |
| A | GLN249 |
| B | ASN252 |
| B | VAL253 |
| B | THR254 |
| B | GLY255 |
| B | GLY256 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ACY D 301 |
| Chain | Residue |
| C | PHE245 |
| C | MET246 |
| C | THR247 |
| C | GLN249 |
| D | ASN252 |
| D | VAL253 |
| D | THR254 |
| D | GLY255 |
| D | GLY256 |
| D | ARG258 |
| site_id | AC7 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAD C 301 |
| Chain | Residue |
| C | ASN90 |
| C | ALA91 |
| C | GLY92 |
| C | THR141 |
| C | ALA142 |
| C | SER143 |
| C | TYR156 |
| C | LYS160 |
| C | GLY187 |
| C | VAL189 |
| C | THR191 |
| C | MET193 |
| C | ARG196 |
| C | HOH404 |
| C | HOH468 |
| C | HOH481 |
| C | HOH484 |
| C | HOH486 |
| C | HOH554 |
| C | GLY16 |
| C | SER18 |
| C | LYS19 |
| C | GLY20 |
| C | ILE21 |
| C | ASP40 |
| C | LEU41 |
| C | VAL62 |
| C | ASP63 |
| C | VAL64 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ACY C 302 |
| Chain | Residue |
| C | ASN252 |
| C | VAL253 |
| C | THR254 |
| C | GLY255 |
| C | GLY256 |
| C | ARG258 |
| D | PHE245 |
| D | MET246 |
| D | THR247 |
| D | GLN249 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SlaakvgaplLahYSASKFAVfGWTqALA |
| Chain | Residue | Details |
| A | SER143-ALA171 |
