4NEA
1.90 Angstrom resolution crystal structure of betaine aldehyde dehydrogenase (betB) 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 |
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 | THR232 |
| A | GLY233 |
| A | GLY234 |
| A | THR237 |
| A | HIS240 |
| A | ILE241 |
| A | THR154 |
| A | GLU255 |
| A | GLY257 |
| A | CYS289 |
| A | HIS336 |
| A | GLU390 |
| A | PHE392 |
| A | HOH627 |
| A | HOH631 |
| A | HOH811 |
| A | HOH812 |
| A | PRO155 |
| A | HOH843 |
| A | HOH960 |
| A | HOH1077 |
| A | HOH1117 |
| A | HOH1139 |
| A | TRP156 |
| A | ASN157 |
| A | LYS180 |
| A | SER182 |
| A | GLU183 |
| A | ALA212 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K A 502 |
| Chain | Residue |
| A | ILE29 |
| A | ASP97 |
| A | ILE184 |
| A | HOH669 |
| A | HOH735 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K A 503 |
| Chain | Residue |
| A | LYS460 |
| A | GLY463 |
| A | HOH647 |
| C | VAL249 |
| C | ASN251 |
| C | HOH667 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K A 504 |
| Chain | Residue |
| A | VAL249 |
| A | ASN251 |
| A | HOH652 |
| C | LYS460 |
| C | GLY463 |
| C | HOH640 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K A 505 |
| Chain | Residue |
| A | GLU474 |
| A | LEU477 |
| A | HOH610 |
| A | HOH772 |
| A | HOH848 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K A 506 |
| Chain | Residue |
| A | LYS224 |
| A | VAL226 |
| A | ASN248 |
| A | THR250 |
| A | HOH715 |
| A | HOH1144 |
| site_id | AC7 |
| Number of Residues | 36 |
| 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 | SER214 |
| 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 | HIS336 |
| B | LYS339 |
| B | GLU390 |
| B | PHE392 |
| B | HOH613 |
| B | HOH812 |
| B | HOH843 |
| B | HOH890 |
| B | HOH917 |
| B | HOH955 |
| B | HOH1006 |
| B | HOH1090 |
| B | HOH1091 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K B 502 |
| Chain | Residue |
| B | GLY463 |
| B | HOH619 |
| D | VAL249 |
| D | ASN251 |
| D | HOH627 |
| B | LYS460 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K B 503 |
| Chain | Residue |
| B | ILE29 |
| B | ASP97 |
| B | ILE184 |
| B | HOH710 |
| B | HOH967 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K B 504 |
| Chain | Residue |
| B | VAL249 |
| B | ASN251 |
| B | HOH618 |
| D | LYS460 |
| D | GLY463 |
| D | HOH617 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K B 505 |
| Chain | Residue |
| B | GLU474 |
| B | LEU477 |
| B | HOH737 |
| B | HOH901 |
| B | HOH907 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K B 506 |
| Chain | Residue |
| B | LYS224 |
| B | VAL226 |
| B | ASN248 |
| B | THR250 |
| B | HOH611 |
| B | HOH785 |
| site_id | BC4 |
| Number of Residues | 35 |
| 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 | ALA212 |
| C | GLY213 |
| C | SER214 |
| C | GLY217 |
| C | ASP218 |
| C | PHE231 |
| C | THR232 |
| C | GLY233 |
| C | GLY234 |
| C | THR237 |
| C | HIS240 |
| C | ILE241 |
| C | GLU255 |
| C | LEU256 |
| C | GLY257 |
| C | CYS289 |
| C | HIS336 |
| C | LYS339 |
| C | GLU390 |
| C | PHE392 |
| C | HOH627 |
| C | HOH666 |
| C | HOH757 |
| C | HOH816 |
| C | HOH827 |
| C | HOH993 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE K C 502 |
| Chain | Residue |
| C | ILE29 |
| C | ASP97 |
| C | ILE184 |
| C | HOH720 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K C 503 |
| Chain | Residue |
| C | LYS224 |
| C | VAL226 |
| C | ASN248 |
| C | THR250 |
| C | HOH712 |
| C | HOH741 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K C 504 |
| Chain | Residue |
| A | HOH1065 |
| C | GLU474 |
| C | LEU477 |
| C | HOH610 |
| C | HOH851 |
| site_id | BC8 |
| Number of Residues | 36 |
| 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 | ALA212 |
| D | GLY213 |
| D | SER214 |
| D | GLY217 |
| D | ASP218 |
| D | PHE231 |
| D | THR232 |
| D | GLY233 |
| D | GLY234 |
| D | THR237 |
| D | HIS240 |
| D | ILE241 |
| D | GLU255 |
| D | GLY257 |
| D | CYS289 |
| D | HIS336 |
| D | LYS339 |
| D | GLU390 |
| D | PHE392 |
| D | HOH618 |
| D | HOH702 |
| D | HOH805 |
| D | HOH891 |
| D | HOH896 |
| D | HOH931 |
| D | HOH990 |
| D | HOH994 |
| D | HOH1031 |
| site_id | BC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K D 502 |
| Chain | Residue |
| D | LYS224 |
| D | VAL226 |
| D | ASN248 |
| D | THR250 |
| D | HOH603 |
| D | HOH656 |
| site_id | CC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K D 503 |
| Chain | Residue |
| D | GLU474 |
| D | LEU477 |
| D | HOH615 |
| D | HOH870 |
| D | HOH1026 |
| site_id | CC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE K D 504 |
| Chain | Residue |
| D | ILE29 |
| D | ASP97 |
| D | ILE184 |
| D | HOH742 |
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 |
