4ZWL
2.60 Angstrom resolution crystal structure of betaine aldehyde dehydrogenase (betB) H448F/Y450L double mutant from Staphylococcus aureus in complex with NAD+ and BME-free 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 |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
| E | 0006578 | biological_process | amino-acid betaine biosynthetic process |
| E | 0008802 | molecular_function | betaine-aldehyde dehydrogenase (NAD+) activity |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| E | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
| F | 0006578 | biological_process | amino-acid betaine biosynthetic process |
| F | 0008802 | molecular_function | betaine-aldehyde dehydrogenase (NAD+) activity |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| F | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| F | 0046872 | molecular_function | metal ion binding |
| G | 0000166 | molecular_function | nucleotide binding |
| G | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
| G | 0006578 | biological_process | amino-acid betaine biosynthetic process |
| G | 0008802 | molecular_function | betaine-aldehyde dehydrogenase (NAD+) activity |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| G | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| G | 0046872 | molecular_function | metal ion binding |
| H | 0000166 | molecular_function | nucleotide binding |
| H | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
| H | 0006578 | biological_process | amino-acid betaine biosynthetic process |
| H | 0008802 | molecular_function | betaine-aldehyde dehydrogenase (NAD+) activity |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| H | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| H | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 28 |
| Details | binding site for residue NAD A 501 |
| Chain | Residue |
| A | ILE153 |
| A | GLY217 |
| A | ASP218 |
| A | PHE231 |
| A | THR232 |
| A | GLY233 |
| A | GLY234 |
| A | THR237 |
| A | HIS240 |
| A | GLU255 |
| A | LEU256 |
| A | THR154 |
| A | GLY257 |
| A | CYS289 |
| A | GLU390 |
| A | PHE392 |
| A | LEU418 |
| A | TRP456 |
| A | HOH640 |
| A | HOH648 |
| A | HOH677 |
| A | PRO155 |
| A | TRP156 |
| A | GLN162 |
| A | LYS180 |
| A | SER182 |
| A | GLU183 |
| A | GLY213 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 502 |
| Chain | Residue |
| A | ARG10 |
| A | HOH674 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 503 |
| Chain | Residue |
| A | ASN338 |
| A | ARG360 |
| C | LYS243 |
| site_id | AC4 |
| Number of Residues | 31 |
| Details | binding site for residue NAD B 501 |
| Chain | Residue |
| B | ILE153 |
| B | THR154 |
| B | PRO155 |
| B | TRP156 |
| B | ASN157 |
| B | LYS180 |
| B | PRO181 |
| B | SER182 |
| B | GLU183 |
| B | GLY213 |
| B | GLY217 |
| B | ASP218 |
| B | PHE231 |
| B | THR232 |
| B | GLY233 |
| B | GLY234 |
| B | THR237 |
| B | HIS240 |
| B | ILE241 |
| B | GLU255 |
| B | LEU256 |
| B | GLY257 |
| B | CYS289 |
| B | GLU390 |
| B | PHE392 |
| B | TRP456 |
| B | HOH610 |
| B | HOH623 |
| B | HOH638 |
| B | HOH642 |
| B | HOH754 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 502 |
| Chain | Residue |
| B | THR403 |
| B | GLU404 |
| G | LYS304 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 503 |
| Chain | Residue |
| B | ASN338 |
| B | ARG360 |
| H | LYS367 |
| site_id | AC7 |
| Number of Residues | 27 |
| Details | binding site for residue NAD C 501 |
| Chain | Residue |
| C | ILE153 |
| C | THR154 |
| C | PRO155 |
| C | TRP156 |
| C | ASN157 |
| C | LYS180 |
| C | PRO181 |
| C | SER182 |
| C | GLU183 |
| C | GLY213 |
| C | GLY217 |
| C | PHE231 |
| C | THR232 |
| C | GLY233 |
| C | GLY234 |
| C | THR237 |
| C | HIS240 |
| C | GLU255 |
| C | LEU256 |
| C | GLY257 |
| C | CYS289 |
| C | GLU390 |
| C | PHE392 |
| C | TRP456 |
| C | HOH630 |
| C | HOH638 |
| C | HOH664 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 C 502 |
| Chain | Residue |
| G | LYS317 |
| C | PRO202 |
| C | LYS203 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 C 503 |
| Chain | Residue |
| C | THR334 |
| C | ARG337 |
| C | ASN338 |
| C | ARG360 |
| C | HOH640 |
| site_id | AD1 |
| Number of Residues | 27 |
| 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 | PHE231 |
| D | THR232 |
| D | GLY233 |
| D | GLY234 |
| D | THR237 |
| D | HIS240 |
| D | GLU255 |
| D | LEU256 |
| D | GLY257 |
| D | CYS289 |
| D | GLU390 |
| D | PHE392 |
| D | TRP456 |
| D | HOH604 |
| D | HOH613 |
| D | HOH623 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 D 502 |
| Chain | Residue |
| D | ARG337 |
| D | ASN338 |
| D | ARG360 |
| site_id | AD3 |
| Number of Residues | 29 |
| Details | binding site for residue NAD E 501 |
| Chain | Residue |
| E | ILE153 |
| E | THR154 |
| E | PRO155 |
| E | TRP156 |
| E | ASN157 |
| E | GLN162 |
| E | LYS180 |
| E | SER182 |
| E | GLU183 |
| E | GLY213 |
| E | GLY217 |
| E | PHE231 |
| E | THR232 |
| E | GLY233 |
| E | GLY234 |
| E | THR237 |
| E | HIS240 |
| E | ILE241 |
| E | GLU255 |
| E | LEU256 |
| E | GLY257 |
| E | CYS289 |
| E | GLU390 |
| E | PHE392 |
| E | LEU418 |
| E | TRP456 |
| E | HOH618 |
| E | HOH631 |
| E | HOH707 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 E 502 |
| Chain | Residue |
| E | PHE265 |
| E | GLN298 |
| E | GLU404 |
| E | LYS429 |
| site_id | AD5 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 E 503 |
| Chain | Residue |
| E | ASN338 |
| E | ARG360 |
| site_id | AD6 |
| Number of Residues | 28 |
| Details | binding site for residue NAD F 501 |
| Chain | Residue |
| F | ILE153 |
| F | THR154 |
| F | PRO155 |
| F | TRP156 |
| F | LYS180 |
| F | SER182 |
| F | GLU183 |
| F | GLY213 |
| F | GLY217 |
| F | ASP218 |
| F | PHE231 |
| F | THR232 |
| F | GLY233 |
| F | GLY234 |
| F | THR237 |
| F | HIS240 |
| F | GLU255 |
| F | LEU256 |
| F | GLY257 |
| F | CYS289 |
| F | GLU390 |
| F | PHE392 |
| F | TRP456 |
| F | HOH601 |
| F | HOH632 |
| F | HOH667 |
| F | HOH671 |
| F | HOH727 |
| site_id | AD7 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 F 502 |
| Chain | Residue |
| F | LYS243 |
| G | LYS243 |
| site_id | AD8 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 F 503 |
| Chain | Residue |
| F | ASN338 |
| F | ARG360 |
| H | LYS243 |
| site_id | AD9 |
| Number of Residues | 1 |
| Details | binding site for residue SO4 F 504 |
| Chain | Residue |
| F | ARG10 |
| site_id | AE1 |
| Number of Residues | 26 |
| Details | binding site for residue NAD G 501 |
| Chain | Residue |
| G | ILE153 |
| G | THR154 |
| G | PRO155 |
| G | TRP156 |
| G | GLN162 |
| G | LYS180 |
| G | SER182 |
| G | GLU183 |
| G | GLY213 |
| G | GLY217 |
| G | ASP218 |
| G | PHE231 |
| G | THR232 |
| G | GLY233 |
| G | GLY234 |
| G | THR237 |
| G | HIS240 |
| G | GLU255 |
| G | LEU256 |
| G | GLY257 |
| G | CYS289 |
| G | GLU390 |
| G | PHE392 |
| G | LEU418 |
| G | TRP456 |
| G | HOH609 |
| site_id | AE2 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 G 502 |
| Chain | Residue |
| G | THR334 |
| G | ARG337 |
| G | ASN338 |
| G | ARG360 |
| site_id | AE3 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 G 503 |
| Chain | Residue |
| C | ARG57 |
| G | LYS314 |
| site_id | AE4 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 G 504 |
| Chain | Residue |
| D | SER342 |
| G | ARG385 |
| G | HOH647 |
| site_id | AE5 |
| Number of Residues | 27 |
| Details | binding site for residue NAD H 501 |
| Chain | Residue |
| H | ILE153 |
| H | THR154 |
| H | PRO155 |
| H | TRP156 |
| H | ASN157 |
| H | GLN162 |
| H | LYS180 |
| H | SER182 |
| H | GLU183 |
| H | GLY213 |
| H | GLY217 |
| H | PHE231 |
| H | THR232 |
| H | GLY233 |
| H | GLY234 |
| H | THR237 |
| H | HIS240 |
| H | GLU255 |
| H | LEU256 |
| H | GLY257 |
| H | CYS289 |
| H | GLU390 |
| H | PHE392 |
| H | LEU418 |
| H | TRP456 |
| H | HOH603 |
| H | HOH618 |
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 |
