5EZ4
2.11 Angstrom resolution crystal structure of betaine aldehyde dehydrogenase (betB) P449M/Y450L double 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 | 32 |
| 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 | LYS339 |
| A | GLU390 |
| A | PHE392 |
| A | HOH619 |
| A | HOH633 |
| A | HOH665 |
| A | HOH755 |
| A | HOH819 |
| A | PRO155 |
| A | HOH901 |
| A | HOH922 |
| A | HOH957 |
| 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 | HOH866 |
| B | VAL249 |
| B | HOH984 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue PGE A 503 |
| Chain | Residue |
| A | HIS448 |
| A | HOH961 |
| 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 | GLU197 |
| A | GLU198 |
| A | HOH632 |
| A | HOH743 |
| A | HOH934 |
| A | HOH1007 |
| B | ASP266 |
| B | ASP267 |
| B | LYS425 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | binding site for residue EPE A 505 |
| Chain | Residue |
| A | ASN492 |
| A | TRP493 |
| A | PHE494 |
| A | SER495 |
| A | LYS496 |
| B | ALA324 |
| B | THR326 |
| B | GLU327 |
| B | HOH659 |
| site_id | AC6 |
| Number of Residues | 34 |
| 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 | LEU256 |
| B | GLY257 |
| B | CME289 |
| B | HIS336 |
| B | LYS339 |
| B | GLU390 |
| B | PHE392 |
| B | HOH629 |
| B | HOH631 |
| B | HOH671 |
| B | HOH676 |
| B | HOH713 |
| B | HOH764 |
| B | HOH887 |
| B | HOH911 |
| B | HOH955 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue NA B 502 |
| Chain | Residue |
| B | HOH906 |
| A | VAL249 |
| A | HOH996 |
| B | LYS460 |
| B | GLY463 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | binding site for residue PGE B 503 |
| Chain | Residue |
| B | HIS448 |
| site_id | AC9 |
| Number of Residues | 12 |
| Details | binding site for residue EPE B 504 |
| Chain | Residue |
| A | ASP266 |
| A | LYS425 |
| A | HOH691 |
| B | SER8 |
| B | TRP17 |
| B | ARG191 |
| B | GLU194 |
| B | GLU198 |
| B | HOH664 |
| B | HOH727 |
| B | HOH766 |
| B | HOH837 |
| site_id | AD1 |
| Number of Residues | 10 |
| Details | binding site for residue EPE B 505 |
| Chain | Residue |
| A | GLU103 |
| A | ALA324 |
| A | THR326 |
| A | GLU327 |
| A | HOH700 |
| B | ASN492 |
| B | TRP493 |
| B | PHE494 |
| B | SER495 |
| B | LYS496 |
| site_id | AD2 |
| Number of Residues | 33 |
| 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 | LYS339 |
| C | GLU390 |
| C | PHE392 |
| C | HOH628 |
| C | HOH660 |
| C | HOH700 |
| C | HOH726 |
| C | HOH802 |
| C | HOH841 |
| C | HOH898 |
| C | HOH933 |
| C | HOH969 |
| C | HOH970 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue NA C 502 |
| Chain | Residue |
| C | LYS460 |
| C | GLY463 |
| C | HOH818 |
| D | VAL249 |
| D | HOH1005 |
| site_id | AD4 |
| Number of Residues | 1 |
| Details | binding site for residue PGE C 503 |
| Chain | Residue |
| C | HOH781 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue PGE C 504 |
| Chain | Residue |
| C | SER342 |
| C | TYR343 |
| C | VAL346 |
| C | ARG385 |
| C | HOH730 |
| D | ASN247 |
| site_id | AD6 |
| Number of Residues | 11 |
| Details | binding site for residue EPE C 505 |
| Chain | Residue |
| B | ASP362 |
| C | ASN492 |
| C | TRP493 |
| C | PHE494 |
| C | SER495 |
| C | LYS496 |
| C | HOH643 |
| D | GLU103 |
| D | ALA324 |
| D | THR326 |
| D | HOH737 |
| site_id | AD7 |
| Number of Residues | 35 |
| Details | binding site for residue NAD D 501 |
| Chain | Residue |
| D | ILE153 |
| D | THR154 |
| D | PRO155 |
| D | TRP156 |
| D | ASN157 |
| D | GLN162 |
| 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 | HIS336 |
| D | LYS339 |
| D | GLU390 |
| D | PHE392 |
| D | HOH613 |
| D | HOH623 |
| D | HOH641 |
| D | HOH657 |
| D | HOH681 |
| D | HOH711 |
| D | HOH854 |
| D | HOH951 |
| D | HOH966 |
| site_id | AD8 |
| Number of Residues | 5 |
| Details | binding site for residue NA D 502 |
| Chain | Residue |
| C | VAL249 |
| C | HOH1017 |
| D | LYS460 |
| D | GLY463 |
| D | HOH884 |
| site_id | AD9 |
| Number of Residues | 4 |
| Details | binding site for residue PGE D 503 |
| Chain | Residue |
| D | TYR158 |
| D | HIS448 |
| D | HOH646 |
| D | HOH918 |
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 |
