6WSB
Crystal structure of a betaine aldehyde dehydrogenase from Burkholderia pseudomallei bound to cofactor NAD
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008802 | molecular_function | betaine-aldehyde dehydrogenase 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 | 0019145 | molecular_function | aminobutyraldehyde dehydrogenase activity |
| A | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047105 | molecular_function | 4-trimethylammoniobutyraldehyde dehydrogenase activity |
| B | 0008802 | molecular_function | betaine-aldehyde dehydrogenase 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 | 0019145 | molecular_function | aminobutyraldehyde dehydrogenase activity |
| B | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047105 | molecular_function | 4-trimethylammoniobutyraldehyde dehydrogenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 35 |
| Details | binding site for residue NAD A 501 |
| Chain | Residue |
| A | ILE149 |
| A | GLY209 |
| A | GLY212 |
| A | ALA213 |
| A | PHE226 |
| A | THR227 |
| A | GLY228 |
| A | GLY229 |
| A | THR232 |
| A | LYS235 |
| A | VAL236 |
| A | GLY150 |
| A | GLU251 |
| A | LEU252 |
| A | GLY253 |
| A | CYS285 |
| A | GLU386 |
| A | PHE388 |
| A | HOH601 |
| A | HOH608 |
| A | HOH618 |
| A | HOH743 |
| A | ALA151 |
| A | HOH772 |
| A | HOH787 |
| A | HOH826 |
| A | HOH888 |
| A | HOH1001 |
| A | HOH1033 |
| A | TRP152 |
| A | ASN153 |
| A | LYS176 |
| A | SER178 |
| A | GLU179 |
| A | ASP208 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue GOL A 502 |
| Chain | Residue |
| A | LEU6 |
| A | ARG8 |
| A | HIS15 |
| A | HOH773 |
| A | HOH927 |
| A | HOH1057 |
| B | TYR4 |
| B | GLY5 |
| B | LEU6 |
| B | GLN7 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 502 |
| Chain | Residue |
| A | SER2 |
| A | GLY5 |
| A | ARG37 |
| B | ASP17 |
| B | GLN39 |
| site_id | AC4 |
| Number of Residues | 35 |
| Details | binding site for Di-peptide NAD B 501 and CYS B 285 |
| Chain | Residue |
| B | ILE149 |
| B | GLY150 |
| B | TRP152 |
| B | ASN153 |
| B | LYS176 |
| B | SER178 |
| B | GLU179 |
| B | ASP208 |
| B | GLY209 |
| B | GLY212 |
| B | ALA213 |
| B | PHE226 |
| B | THR227 |
| B | GLY228 |
| B | GLY229 |
| B | THR232 |
| B | VAL236 |
| B | GLU251 |
| B | LEU252 |
| B | GLY253 |
| B | VAL284 |
| B | THR286 |
| B | ASN287 |
| B | GLU386 |
| B | PHE388 |
| B | LEU414 |
| B | HOH601 |
| B | HOH630 |
| B | HOH652 |
| B | HOH791 |
| B | HOH883 |
| B | HOH929 |
| B | HOH951 |
| B | HOH1009 |
| B | HOH1066 |
| site_id | AC5 |
| Number of Residues | 35 |
| Details | binding site for Di-peptide NAD B 501 and CYS B 285 |
| Chain | Residue |
| B | GLY229 |
| B | THR232 |
| B | VAL236 |
| B | GLU251 |
| B | LEU252 |
| B | GLY253 |
| B | VAL284 |
| B | THR286 |
| B | ASN287 |
| B | GLU386 |
| B | PHE388 |
| B | LEU414 |
| B | HOH601 |
| B | HOH630 |
| B | HOH652 |
| B | HOH791 |
| B | HOH883 |
| B | HOH929 |
| B | HOH951 |
| B | HOH1009 |
| B | HOH1066 |
| B | ILE149 |
| B | GLY150 |
| B | TRP152 |
| B | ASN153 |
| B | LYS176 |
| B | SER178 |
| B | GLU179 |
| B | ASP208 |
| B | GLY209 |
| B | GLY212 |
| B | ALA213 |
| B | PHE226 |
| B | THR227 |
| B | GLY228 |
Functional Information from PROSITE/UniProt
| site_id | PS00070 |
| Number of Residues | 12 |
| Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FfSAGQVCTNGT |
| Chain | Residue | Details |
| A | PHE278-THR289 |
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. MELGGKSP |
| Chain | Residue | Details |
| A | MET250-PRO257 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Charge relay system => ECO:0000255|HAMAP-Rule:MF_00804 |
| Chain | Residue | Details |
| A | LYS162 | |
| A | GLU463 | |
| B | LYS162 | |
| B | GLU463 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00804 |
| Chain | Residue | Details |
| A | GLU251 | |
| B | GLU251 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_00804 |
| Chain | Residue | Details |
| A | CYS285 | |
| B | CYS285 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00804 |
| Chain | Residue | Details |
| A | VAL180 | |
| A | LEU245 | |
| A | LYS456 | |
| A | GLY459 | |
| B | THR26 | |
| B | ASP93 | |
| B | VAL180 | |
| B | LEU245 | |
| B | LYS456 | |
| B | GLY459 | |
| A | THR26 | |
| A | ASP93 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00804, ECO:0007744|PDB:6WSB |
| Chain | Residue | Details |
| A | GLU386 | |
| B | GLY150 | |
| B | LYS176 | |
| B | GLY229 | |
| B | GLY253 | |
| B | GLU386 | |
| A | GLY150 | |
| A | LYS176 | |
| A | GLY229 | |
| A | GLY253 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | BINDING: covalent => ECO:0000255|HAMAP-Rule:MF_00804, ECO:0007744|PDB:6WSB |
| Chain | Residue | Details |
| A | CYS285 | |
| B | CYS285 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | SITE: Seems to be a necessary countercharge to the potassium cations => ECO:0000255|HAMAP-Rule:MF_00804 |
| Chain | Residue | Details |
| A | GLU247 | |
| B | GLU247 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | MOD_RES: Cysteine sulfenic acid (-SOH) => ECO:0000255|HAMAP-Rule:MF_00804 |
| Chain | Residue | Details |
| A | CYS285 | |
| B | CYS285 |
