4WEO
Crystal Structure of a Putative acetoin(Diacetyl) Reductase Burkholderia cenocepacia
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 0030497 | biological_process | fatty acid elongation |
| 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 | 0030497 | biological_process | fatty acid elongation |
| 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 | 0030497 | biological_process | fatty acid elongation |
| 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 | 0030497 | biological_process | fatty acid elongation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 301 |
| Chain | Residue |
| A | GLN247 |
| A | ALA248 |
| D | ALA248 |
| D | VAL249 |
| D | ASN250 |
| D | PHE257 |
| D | EDO301 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 302 |
| Chain | Residue |
| A | GLY223 |
| C | ALA46 |
| C | ARG49 |
| A | LEU217 |
| A | ILE220 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue EDO B 301 |
| Chain | Residue |
| B | ARG233 |
| B | PHE237 |
| B | THR240 |
| B | HOH433 |
| B | HOH437 |
| C | ARG233 |
| C | PHE237 |
| C | HOH487 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 302 |
| Chain | Residue |
| A | PHE150 |
| A | PRO151 |
| B | LYS172 |
| B | HOH512 |
| B | HOH543 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue EDO C 301 |
| Chain | Residue |
| B | ALA248 |
| B | VAL249 |
| B | ASN250 |
| B | PHE257 |
| C | GLN247 |
| C | ALA248 |
| C | EDO302 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue EDO C 302 |
| Chain | Residue |
| B | GLN247 |
| B | ALA248 |
| C | ALA248 |
| C | VAL249 |
| C | ASN250 |
| C | PHE257 |
| C | EDO301 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue GOL C 303 |
| Chain | Residue |
| C | ARG190 |
| C | THR191 |
| C | GLN210 |
| D | GLN133 |
| D | ARG135 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue MG C 304 |
| Chain | Residue |
| C | HOH403 |
| C | HOH406 |
| C | HOH424 |
| C | HOH449 |
| D | HOH407 |
| D | HOH409 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue EDO D 301 |
| Chain | Residue |
| A | ALA248 |
| A | VAL249 |
| A | ASN250 |
| A | PHE257 |
| A | EDO301 |
| D | GLN247 |
| D | ALA248 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue EDO D 302 |
| Chain | Residue |
| C | ARG176 |
| D | ARG17 |
| D | GLY18 |
| D | ARG21 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue GOL D 303 |
| Chain | Residue |
| C | GLN133 |
| C | ARG135 |
| D | ARG190 |
| D | THR191 |
| D | GLN210 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue MG D 304 |
| Chain | Residue |
| C | HOH401 |
| C | HOH415 |
| D | HOH405 |
| D | HOH411 |
| D | HOH419 |
| D | HOH441 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue CL D 305 |
| Chain | Residue |
| C | HOH423 |
| C | HOH434 |
| D | ALA225 |
| D | HOH420 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SiagkegfpnLahYSASKFAVvGFTnALA |
| Chain | Residue | Details |
| A | SER143-ALA171 |
