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 | 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 | 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 | 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 | 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 |