4O5H
X-ray crystal structure of a putative phenylacetaldehyde dehydrogenase from Burkholderia cenocepacia
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008957 | molecular_function | phenylacetaldehyde dehydrogenase (NAD+) activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| B | 0008957 | molecular_function | phenylacetaldehyde dehydrogenase (NAD+) activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| C | 0008957 | molecular_function | phenylacetaldehyde dehydrogenase (NAD+) activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| D | 0008957 | molecular_function | phenylacetaldehyde dehydrogenase (NAD+) activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 601 |
| Chain | Residue |
| A | ARG88 |
| A | LEU91 |
| A | VAL92 |
| A | EDO604 |
| C | ASP95 |
| C | HOH831 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 602 |
| Chain | Residue |
| A | TYR502 |
| A | HOH916 |
| A | HOH1046 |
| A | HOH1129 |
| A | HOH1179 |
| A | HOH1205 |
| A | SER156 |
| A | GLU157 |
| A | ILE158 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 603 |
| Chain | Residue |
| A | GLY233 |
| A | GLY237 |
| A | ILE261 |
| A | HOH783 |
| A | HOH1135 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 604 |
| Chain | Residue |
| A | ASP95 |
| A | GOL601 |
| A | HOH734 |
| C | ARG88 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 605 |
| Chain | Residue |
| A | VAL43 |
| A | ASP111 |
| A | ASP204 |
| A | HOH716 |
| A | HOH764 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 601 |
| Chain | Residue |
| B | ASN100 |
| B | ARG211 |
| B | HOH777 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 602 |
| Chain | Residue |
| B | VAL43 |
| B | ASP111 |
| B | ASP204 |
| B | HOH707 |
| B | HOH955 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL C 601 |
| Chain | Residue |
| C | PRO22 |
| C | GLN24 |
| C | GLU214 |
| C | HOH1127 |
| C | HOH1188 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA C 602 |
| Chain | Residue |
| C | VAL43 |
| C | ASP111 |
| C | ASP204 |
| C | HOH781 |
| C | HOH833 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL D 601 |
| Chain | Residue |
| D | ASN100 |
| D | ARG211 |
| D | LEU215 |
| D | HOH1173 |
| site_id | BC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL D 602 |
| Chain | Residue |
| D | ALA298 |
| D | ASN299 |
| D | PHE302 |
| D | PHE303 |
| D | LEU336 |
| D | GLN347 |
| D | HOH946 |
| D | HOH969 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA D 603 |
| Chain | Residue |
| D | VAL43 |
| D | ASP111 |
| D | ASP204 |
| D | HOH850 |
| D | HOH895 |
Functional Information from PROSITE/UniProt
| site_id | PS00070 |
| Number of Residues | 12 |
| Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FfNQGQVCTAGS |
| Chain | Residue | Details |
| A | PHE302-SER313 |
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKSP |
| Chain | Residue | Details |
| A | LEU274-PRO281 |
