5DIB
2.25 Angstrom resolution crystal structure of betaine aldehyde dehydrogenase (betB) Y450L point mutant from Staphylococcus aureus in complex with NAD+ and BME-modified Cys289
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
| A | 0006578 | biological_process | amino-acid betaine biosynthetic process |
| A | 0008802 | molecular_function | betaine-aldehyde 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 | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
| B | 0006578 | biological_process | amino-acid betaine biosynthetic process |
| B | 0008802 | molecular_function | betaine-aldehyde 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 | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
| C | 0006578 | biological_process | amino-acid betaine biosynthetic process |
| C | 0008802 | molecular_function | betaine-aldehyde 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 | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
| D | 0006578 | biological_process | amino-acid betaine biosynthetic process |
| D | 0008802 | molecular_function | betaine-aldehyde 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 | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | binding site for residue NAD A 501 |
| Chain | Residue |
| A | ILE153 |
| A | GLY217 |
| A | ASP218 |
| A | PHE231 |
| A | GLY233 |
| A | GLY234 |
| A | THR237 |
| A | HIS240 |
| A | ILE241 |
| A | LEU256 |
| A | GLY257 |
| A | THR154 |
| A | CME289 |
| A | LYS339 |
| A | GLU390 |
| A | PHE392 |
| A | HOH674 |
| A | PRO155 |
| A | TRP156 |
| A | ASN157 |
| A | LYS180 |
| A | SER182 |
| A | GLU183 |
| A | GLY213 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 502 |
| Chain | Residue |
| A | ILE29 |
| A | ASP97 |
| A | ILE184 |
| A | THR185 |
| A | HOH779 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | binding site for residue EPE A 503 |
| Chain | Residue |
| A | SER8 |
| A | TRP17 |
| A | ARG191 |
| A | GLU194 |
| A | GLU198 |
| A | HOH616 |
| A | HOH692 |
| B | ASP266 |
| B | ASP267 |
| B | LYS425 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue EPE A 504 |
| Chain | Residue |
| A | ASP266 |
| A | ASP267 |
| A | LYS425 |
| A | HOH626 |
| B | SER8 |
| B | ARG191 |
| B | GLU194 |
| B | GLU198 |
| B | HOH666 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 505 |
| Chain | Residue |
| A | VAL249 |
| A | HOH796 |
| B | LYS460 |
| B | GLY463 |
| B | HOH738 |
| site_id | AC6 |
| Number of Residues | 25 |
| Details | binding site for residue NAD B 501 |
| Chain | Residue |
| B | ILE153 |
| B | THR154 |
| B | PRO155 |
| B | TRP156 |
| B | ASN157 |
| B | LYS180 |
| B | SER182 |
| B | GLU183 |
| B | GLY213 |
| B | GLY217 |
| B | ASP218 |
| B | PHE231 |
| B | GLY233 |
| B | GLY234 |
| B | THR237 |
| B | HIS240 |
| B | GLU255 |
| B | LEU256 |
| B | GLY257 |
| B | CME289 |
| B | LYS339 |
| B | GLU390 |
| B | PHE392 |
| B | HOH647 |
| B | HOH743 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue NA B 502 |
| Chain | Residue |
| B | ILE29 |
| B | ASP97 |
| B | ILE184 |
| B | HOH649 |
| B | HOH791 |
| site_id | AC8 |
| Number of Residues | 25 |
| Details | binding site for residue NAD C 501 |
| Chain | Residue |
| C | GLY257 |
| C | CME289 |
| C | LYS339 |
| C | GLU390 |
| C | PHE392 |
| C | HOH604 |
| C | HOH655 |
| C | HOH754 |
| C | HOH769 |
| C | ILE153 |
| C | THR154 |
| C | PRO155 |
| C | TRP156 |
| C | ASN157 |
| C | LYS180 |
| C | SER182 |
| C | GLU183 |
| C | GLY213 |
| C | GLY217 |
| C | PHE231 |
| C | GLY233 |
| C | GLY234 |
| C | THR237 |
| C | HIS240 |
| C | GLU255 |
| site_id | AC9 |
| Number of Residues | 28 |
| Details | binding site for residue NAD D 501 |
| Chain | Residue |
| D | ILE153 |
| D | THR154 |
| D | PRO155 |
| D | TRP156 |
| D | ASN157 |
| D | LYS180 |
| D | SER182 |
| D | GLU183 |
| D | GLY213 |
| D | GLY217 |
| D | ASP218 |
| D | PHE231 |
| D | GLY233 |
| D | GLY234 |
| D | THR237 |
| D | HIS240 |
| D | ILE241 |
| D | GLU255 |
| D | LEU256 |
| D | GLY257 |
| D | CME289 |
| D | LYS339 |
| D | GLU390 |
| D | PHE392 |
| D | HOH603 |
| D | HOH609 |
| D | HOH711 |
| D | HOH759 |
Functional Information from PROSITE/UniProt
| site_id | PS00070 |
| Number of Residues | 12 |
| Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. YfHAGQVCSAGS |
| Chain | Residue | Details |
| A | TYR282-SER293 |
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKNP |
| Chain | Residue | Details |
| A | LEU254-PRO261 |
