5KF0
Crystal structure of an Aldedhyde dehydrogenase from Burkholderia vietnamiensis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0008911 | molecular_function | lactaldehyde 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 |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0008911 | molecular_function | lactaldehyde 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 |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0008911 | molecular_function | lactaldehyde 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 |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0008911 | molecular_function | lactaldehyde 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 |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 36 |
| Details | binding site for residue NDP A 501 |
| Chain | Residue |
| A | ILE150 |
| A | ARG181 |
| A | ALA208 |
| A | ARG210 |
| A | ALA213 |
| A | PHE227 |
| A | THR228 |
| A | GLY229 |
| A | SER230 |
| A | PRO231 |
| A | VAL233 |
| A | SER151 |
| A | GLU249 |
| A | LEU250 |
| A | GLY251 |
| A | CYS285 |
| A | GLU379 |
| A | PHE381 |
| A | TYR446 |
| A | HOH616 |
| A | HOH665 |
| A | HOH682 |
| A | PRO152 |
| A | HOH692 |
| A | HOH717 |
| A | HOH776 |
| A | HOH783 |
| A | HOH791 |
| A | HOH891 |
| A | HOH945 |
| A | PHE153 |
| A | ASN154 |
| A | LEU159 |
| A | LYS177 |
| A | ALA179 |
| A | SER180 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 502 |
| Chain | Residue |
| A | HIS-2 |
| A | HIS0 |
| A | GLU85 |
| B | GLU13 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue MRD A 503 |
| Chain | Residue |
| A | ALA67 |
| A | GLU195 |
| A | THR196 |
| A | ASN197 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue ACT A 504 |
| Chain | Residue |
| A | ARG104 |
| A | PHE155 |
| A | CYS285 |
| A | ILE286 |
| A | ARG440 |
| A | TYR446 |
| A | HOH610 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue MPD A 505 |
| Chain | Residue |
| A | ASP271 |
| A | PHE275 |
| A | LYS308 |
| A | HOH881 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue MPD A 506 |
| Chain | Residue |
| A | LYS450 |
| A | ASP451 |
| A | HOH650 |
| B | GLU220 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue MPD A 507 |
| Chain | Residue |
| A | ILE119 |
| A | ARG140 |
| A | HOH688 |
| A | HOH718 |
| A | HOH850 |
| B | TRP423 |
| D | ASN125 |
| D | THR136 |
| site_id | AC8 |
| Number of Residues | 37 |
| Details | binding site for residue NDP B 501 |
| Chain | Residue |
| B | HOH775 |
| B | HOH796 |
| B | HOH808 |
| B | HOH820 |
| B | HOH975 |
| B | ILE150 |
| B | SER151 |
| B | PRO152 |
| B | PHE153 |
| B | ASN154 |
| B | LEU159 |
| B | LYS177 |
| B | PRO178 |
| B | ALA179 |
| B | SER180 |
| B | ARG181 |
| B | ALA208 |
| B | ARG210 |
| B | ALA213 |
| B | PHE227 |
| B | THR228 |
| B | GLY229 |
| B | SER230 |
| B | PRO231 |
| B | VAL233 |
| B | GLU249 |
| B | LEU250 |
| B | GLY251 |
| B | CYS285 |
| B | GLU379 |
| B | PHE381 |
| B | TYR446 |
| B | HOH661 |
| B | HOH695 |
| B | HOH698 |
| B | HOH706 |
| B | HOH715 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue ACT B 502 |
| Chain | Residue |
| B | ARG64 |
| B | VAL68 |
| B | ASN197 |
| B | LEU198 |
| B | MRD503 |
| B | HOH647 |
| B | HOH869 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue MRD B 503 |
| Chain | Residue |
| B | ARG64 |
| B | ALA67 |
| B | GLU195 |
| B | THR196 |
| B | ASN197 |
| B | ACT502 |
| site_id | AD2 |
| Number of Residues | 9 |
| Details | binding site for residue MPD B 504 |
| Chain | Residue |
| B | VAL123 |
| B | ASN125 |
| B | THR136 |
| B | HOH709 |
| C | ILE119 |
| C | ARG140 |
| C | HOH913 |
| D | TRP423 |
| D | HOH819 |
| site_id | AD3 |
| Number of Residues | 7 |
| Details | binding site for residue ACT B 505 |
| Chain | Residue |
| B | ARG104 |
| B | PHE155 |
| B | CYS285 |
| B | ARG440 |
| B | TYR446 |
| B | HOH610 |
| B | HOH682 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue MPD B 506 |
| Chain | Residue |
| B | ASP271 |
| B | PHE275 |
| B | LYS308 |
| B | PHE323 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue MPD B 507 |
| Chain | Residue |
| A | GLU220 |
| A | LYS243 |
| B | LYS450 |
| B | ASP451 |
| B | HOH686 |
| site_id | AD6 |
| Number of Residues | 2 |
| Details | binding site for residue MPD B 508 |
| Chain | Residue |
| D | PHE263 |
| D | LEU297 |
| site_id | AD7 |
| Number of Residues | 5 |
| Details | binding site for residue MPD B 509 |
| Chain | Residue |
| A | TRP423 |
| B | ARG140 |
| B | HOH636 |
| B | HOH654 |
| C | THR136 |
| site_id | AD8 |
| Number of Residues | 36 |
| Details | binding site for residue NDP C 501 |
| Chain | Residue |
| C | ILE150 |
| C | SER151 |
| C | PRO152 |
| C | PHE153 |
| C | ASN154 |
| C | LEU159 |
| C | LYS177 |
| C | ALA179 |
| C | SER180 |
| C | ARG181 |
| C | ALA208 |
| C | ARG210 |
| C | ALA213 |
| C | PHE227 |
| C | THR228 |
| C | GLY229 |
| C | SER230 |
| C | PRO231 |
| C | VAL233 |
| C | GLU249 |
| C | LEU250 |
| C | GLY251 |
| C | CYS285 |
| C | GLU379 |
| C | PHE381 |
| C | TYR446 |
| C | HOH654 |
| C | HOH663 |
| C | HOH665 |
| C | HOH674 |
| C | HOH718 |
| C | HOH735 |
| C | HOH793 |
| C | HOH883 |
| C | HOH890 |
| C | HOH907 |
| site_id | AD9 |
| Number of Residues | 7 |
| Details | binding site for residue ACT C 502 |
| Chain | Residue |
| C | ARG64 |
| C | VAL68 |
| C | ASN197 |
| C | LEU198 |
| C | MRD503 |
| C | HOH672 |
| C | HOH689 |
| site_id | AE1 |
| Number of Residues | 6 |
| Details | binding site for residue MRD C 503 |
| Chain | Residue |
| C | ARG64 |
| C | ALA67 |
| C | GLU195 |
| C | THR196 |
| C | ASN197 |
| C | ACT502 |
| site_id | AE2 |
| Number of Residues | 6 |
| Details | binding site for residue ACT C 504 |
| Chain | Residue |
| C | ARG104 |
| C | CYS285 |
| C | ILE286 |
| C | ARG440 |
| C | TYR446 |
| C | HOH601 |
| site_id | AE3 |
| Number of Residues | 3 |
| Details | binding site for residue MPD C 505 |
| Chain | Residue |
| C | ASP271 |
| C | PHE275 |
| C | LYS308 |
| site_id | AE4 |
| Number of Residues | 5 |
| Details | binding site for residue MPD C 506 |
| Chain | Residue |
| C | LYS450 |
| C | ASP451 |
| C | HOH628 |
| D | GLU220 |
| D | ARG223 |
| site_id | AE5 |
| Number of Residues | 6 |
| Details | binding site for residue MPD D 501 |
| Chain | Residue |
| A | THR136 |
| C | TRP423 |
| D | ILE119 |
| D | ARG140 |
| D | HOH626 |
| D | HOH666 |
| site_id | AE6 |
| Number of Residues | 7 |
| Details | binding site for residue MPD D 502 |
| Chain | Residue |
| A | TYR138 |
| A | MET472 |
| B | ALA419 |
| B | GLN420 |
| C | GLN420 |
| D | TYR138 |
| D | MET472 |
| site_id | AE7 |
| Number of Residues | 36 |
| Details | binding site for residue NDP D 503 |
| Chain | Residue |
| D | ILE150 |
| D | SER151 |
| D | PRO152 |
| D | PHE153 |
| D | ASN154 |
| D | LEU159 |
| D | LYS177 |
| D | PRO178 |
| D | ALA179 |
| D | SER180 |
| D | ARG181 |
| D | ALA208 |
| D | ARG210 |
| D | ALA213 |
| D | PHE227 |
| D | THR228 |
| D | GLY229 |
| D | SER230 |
| D | PRO231 |
| D | VAL233 |
| D | GLU249 |
| D | LEU250 |
| D | GLY251 |
| D | CYS285 |
| D | GLU379 |
| D | PHE381 |
| D | TYR446 |
| D | HOH660 |
| D | HOH668 |
| D | HOH675 |
| D | HOH686 |
| D | HOH694 |
| D | HOH711 |
| D | HOH760 |
| D | HOH799 |
| D | HOH912 |
| site_id | AE8 |
| Number of Residues | 6 |
| Details | binding site for residue ACT D 504 |
| Chain | Residue |
| D | ARG64 |
| D | VAL68 |
| D | ASN197 |
| D | LEU198 |
| D | MRD505 |
| D | HOH617 |
| site_id | AE9 |
| Number of Residues | 5 |
| Details | binding site for residue MRD D 505 |
| Chain | Residue |
| D | ALA67 |
| D | GLU195 |
| D | THR196 |
| D | ASN197 |
| D | ACT504 |
| site_id | AF1 |
| Number of Residues | 6 |
| Details | binding site for residue ACT D 506 |
| Chain | Residue |
| D | ARG104 |
| D | CYS285 |
| D | ARG440 |
| D | TYR446 |
| D | HOH602 |
| D | HOH621 |
| site_id | AF2 |
| Number of Residues | 3 |
| Details | binding site for residue MPD D 507 |
| Chain | Residue |
| D | ASP271 |
| D | PHE275 |
| D | LYS308 |
| site_id | AF3 |
| Number of Residues | 6 |
| Details | binding site for residue MRD D 508 |
| Chain | Residue |
| C | GLU220 |
| C | ARG223 |
| C | LYS243 |
| D | LYS450 |
| D | ASP451 |
| D | HOH671 |
Functional Information from PROSITE/UniProt
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGNAA |
| Chain | Residue | Details |
| A | LEU248-ALA255 |
