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 | 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 | 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 |