5EYU
1.72 Angstrom resolution crystal structure of betaine aldehyde dehydrogenase (betB) P449M 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 | 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 | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070887 | biological_process | cellular response to chemical stimulus |
| B | 0000166 | molecular_function | nucleotide binding |
| 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 | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0070887 | biological_process | cellular response to chemical stimulus |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0008802 | molecular_function | betaine-aldehyde dehydrogenase 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 |
| C | 0070887 | biological_process | cellular response to chemical stimulus |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0008802 | molecular_function | betaine-aldehyde dehydrogenase 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 |
| D | 0070887 | biological_process | cellular response to chemical stimulus |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 34 |
| Details | binding site for residue NAD A 501 |
| Chain | Residue |
| A | ILE153 |
| A | GLY213 |
| A | GLY217 |
| A | ASP218 |
| A | PHE231 |
| A | GLY233 |
| A | GLY234 |
| A | THR237 |
| A | HIS240 |
| A | ILE241 |
| A | GLU255 |
| A | THR154 |
| A | GLY257 |
| A | CME289 |
| A | HIS336 |
| A | GLU390 |
| A | PHE392 |
| A | HOH660 |
| A | HOH672 |
| A | HOH725 |
| A | HOH778 |
| A | HOH796 |
| A | PRO155 |
| A | HOH904 |
| A | HOH926 |
| A | HOH954 |
| A | HOH989 |
| A | HOH1016 |
| A | TRP156 |
| A | ASN157 |
| A | GLN162 |
| A | LYS180 |
| A | SER182 |
| A | GLU183 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 502 |
| Chain | Residue |
| A | LYS460 |
| A | GLY463 |
| A | HOH961 |
| B | VAL249 |
| B | HOH1052 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue NA A 503 |
| Chain | Residue |
| A | ILE29 |
| A | ASP97 |
| A | ILE184 |
| A | HOH1049 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | binding site for residue EPE A 504 |
| Chain | Residue |
| A | SER8 |
| A | TRP17 |
| A | ARG191 |
| A | GLU194 |
| A | GLU198 |
| A | HOH627 |
| A | HOH691 |
| A | HOH929 |
| A | HOH951 |
| A | HOH975 |
| B | ASP266 |
| B | ASP267 |
| B | LYS425 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue PGE A 505 |
| Chain | Residue |
| A | TYR450 |
| A | HOH618 |
| A | HOH649 |
| A | HOH772 |
| A | HOH1021 |
| site_id | AC6 |
| Number of Residues | 32 |
| 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 | ILE241 |
| B | GLU255 |
| B | GLY257 |
| B | CME289 |
| B | HIS336 |
| B | GLU390 |
| B | PHE392 |
| B | HOH625 |
| B | HOH638 |
| B | HOH661 |
| B | HOH670 |
| B | HOH853 |
| B | HOH885 |
| B | HOH938 |
| B | HOH967 |
| B | HOH1012 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue NA B 502 |
| Chain | Residue |
| A | VAL249 |
| A | HOH1047 |
| B | LYS460 |
| B | GLY463 |
| B | HOH939 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue NA B 503 |
| Chain | Residue |
| B | ASP97 |
| B | ILE184 |
| B | HOH1044 |
| B | ILE29 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | binding site for residue EPE B 504 |
| Chain | Residue |
| A | ASP266 |
| A | LYS425 |
| B | SER8 |
| B | TRP17 |
| B | ARG191 |
| B | GLU194 |
| B | GLU198 |
| B | HOH613 |
| B | HOH848 |
| B | HOH851 |
| B | HOH1146 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue EPE B 505 |
| Chain | Residue |
| A | ALA324 |
| A | THR326 |
| B | ASN492 |
| B | TRP493 |
| B | HOH783 |
| B | HOH812 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue PGE B 506 |
| Chain | Residue |
| B | TYR450 |
| B | HOH734 |
| B | HOH988 |
| site_id | AD3 |
| Number of Residues | 36 |
| Details | binding site for residue NAD C 501 |
| Chain | Residue |
| C | ILE153 |
| C | THR154 |
| C | PRO155 |
| C | TRP156 |
| C | ASN157 |
| C | LYS180 |
| C | SER182 |
| C | GLU183 |
| C | GLY213 |
| C | GLY217 |
| C | ASP218 |
| C | PHE231 |
| C | GLY233 |
| C | GLY234 |
| C | THR237 |
| C | HIS240 |
| C | ILE241 |
| C | GLU255 |
| C | GLY257 |
| C | CME289 |
| C | HIS336 |
| C | GLU390 |
| C | PHE392 |
| C | HOH624 |
| C | HOH627 |
| C | HOH643 |
| C | HOH678 |
| C | HOH721 |
| C | HOH728 |
| C | HOH765 |
| C | HOH808 |
| C | HOH836 |
| C | HOH837 |
| C | HOH899 |
| C | HOH1002 |
| C | HOH1020 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue NA C 502 |
| Chain | Residue |
| C | LYS460 |
| C | GLY463 |
| C | HOH901 |
| D | VAL249 |
| D | HOH1043 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue NA C 503 |
| Chain | Residue |
| C | ILE29 |
| C | ASP97 |
| C | ILE184 |
| C | HOH1030 |
| site_id | AD6 |
| Number of Residues | 9 |
| Details | binding site for residue EPE C 504 |
| Chain | Residue |
| B | ASP362 |
| C | ASN492 |
| C | TRP493 |
| C | HOH612 |
| C | HOH759 |
| D | ALA324 |
| D | ASP325 |
| D | THR326 |
| D | GLU327 |
| site_id | AD7 |
| Number of Residues | 4 |
| Details | binding site for residue PGE C 505 |
| Chain | Residue |
| C | PHE283 |
| C | TYR450 |
| C | HOH660 |
| C | HOH1039 |
| site_id | AD8 |
| Number of Residues | 33 |
| 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 | GLY257 |
| D | CME289 |
| D | HIS336 |
| D | GLU390 |
| D | PHE392 |
| D | HOH610 |
| D | HOH654 |
| D | HOH671 |
| D | HOH706 |
| D | HOH716 |
| D | HOH719 |
| D | HOH745 |
| D | HOH826 |
| D | HOH846 |
| D | HOH992 |
| site_id | AD9 |
| Number of Residues | 5 |
| Details | binding site for residue NA D 502 |
| Chain | Residue |
| C | VAL249 |
| C | HOH1050 |
| D | LYS460 |
| D | GLY463 |
| D | HOH942 |
| site_id | AE1 |
| Number of Residues | 4 |
| Details | binding site for residue NA D 503 |
| Chain | Residue |
| D | ILE29 |
| D | ASP97 |
| D | ILE184 |
| D | HOH1038 |
| site_id | AE2 |
| Number of Residues | 5 |
| Details | binding site for residue PGE D 504 |
| Chain | Residue |
| D | TYR158 |
| D | TYR450 |
| D | HOH604 |
| D | HOH676 |
| D | HOH919 |
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 |
