4MPY
1.85 Angstrom resolution crystal structure of betaine aldehyde dehydrogenase (betB) from Staphylococcus aureus (IDP00699) in complex with NAD+
Replaces: 3FG0Functional 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 | 33 |
| Details | BINDING SITE FOR RESIDUE NAD A 501 |
| Chain | Residue |
| A | ILE153 |
| A | GLY217 |
| A | PHE231 |
| A | GLY233 |
| A | GLY234 |
| A | THR237 |
| A | HIS240 |
| A | ILE241 |
| A | GLU255 |
| A | GLY257 |
| A | CME289 |
| A | THR154 |
| A | HIS336 |
| A | LYS339 |
| A | GLU390 |
| A | PHE392 |
| A | HOH674 |
| A | HOH724 |
| A | HOH819 |
| A | HOH823 |
| A | HOH867 |
| A | HOH923 |
| A | PRO155 |
| A | HOH973 |
| A | HOH998 |
| A | HOH1030 |
| A | HOH1038 |
| A | TRP156 |
| A | ASN157 |
| A | LYS180 |
| A | SER182 |
| A | GLU183 |
| A | GLY213 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 502 |
| Chain | Residue |
| A | LYS460 |
| A | GLY463 |
| A | HOH648 |
| B | VAL249 |
| B | HOH726 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA A 503 |
| Chain | Residue |
| A | ILE29 |
| A | ASP97 |
| A | ILE184 |
| A | HOH843 |
| site_id | AC4 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE NAD B 501 |
| Chain | Residue |
| B | ILE153 |
| B | THR154 |
| B | PRO155 |
| B | TRP156 |
| B | ASN157 |
| B | GLN162 |
| 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 | GLY257 |
| B | CME289 |
| B | HIS336 |
| B | LYS339 |
| B | GLU390 |
| B | PHE392 |
| B | HOH643 |
| B | HOH649 |
| B | HOH734 |
| B | HOH741 |
| B | HOH809 |
| B | HOH828 |
| B | HOH855 |
| B | HOH859 |
| B | HOH1008 |
| B | HOH1093 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 502 |
| Chain | Residue |
| A | VAL249 |
| A | HOH627 |
| B | LYS460 |
| B | GLY463 |
| B | HOH674 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA B 503 |
| Chain | Residue |
| B | ILE29 |
| B | ASP97 |
| B | ILE184 |
| B | HOH676 |
| site_id | AC7 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE NAD C 501 |
| Chain | Residue |
| C | GLY233 |
| C | GLY234 |
| C | THR237 |
| C | HIS240 |
| C | GLU255 |
| C | GLY257 |
| C | CME289 |
| C | HIS336 |
| C | LYS339 |
| C | GLU390 |
| C | PHE392 |
| C | HOH613 |
| C | HOH663 |
| C | HOH706 |
| C | HOH720 |
| C | HOH745 |
| C | HOH801 |
| C | HOH842 |
| C | HOH929 |
| C | HOH1047 |
| C | HOH1126 |
| C | HOH1159 |
| C | HOH1187 |
| C | ILE153 |
| C | THR154 |
| C | PRO155 |
| C | TRP156 |
| C | ASN157 |
| C | GLN162 |
| C | LYS180 |
| C | SER182 |
| C | GLU183 |
| C | GLY213 |
| C | GLY217 |
| C | ASP218 |
| C | PHE231 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA C 502 |
| Chain | Residue |
| C | LYS460 |
| C | GLY463 |
| C | HOH641 |
| D | VAL249 |
| D | HOH667 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA C 503 |
| Chain | Residue |
| C | ILE28 |
| C | ILE29 |
| C | ASP97 |
| C | ILE184 |
| C | HOH871 |
| site_id | BC1 |
| Number of Residues | 34 |
| 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 | GLY213 |
| D | GLY217 |
| D | ASP218 |
| D | PHE231 |
| D | GLY233 |
| D | GLY234 |
| D | THR237 |
| D | HIS240 |
| D | ILE241 |
| D | GLU255 |
| D | GLY257 |
| D | CME289 |
| D | HIS336 |
| D | LYS339 |
| D | GLU390 |
| D | PHE392 |
| D | HOH630 |
| D | HOH758 |
| D | HOH822 |
| D | HOH873 |
| D | HOH910 |
| D | HOH929 |
| D | HOH1085 |
| D | HOH1124 |
| D | HOH1153 |
| D | HOH1167 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA D 502 |
| Chain | Residue |
| C | VAL249 |
| C | HOH718 |
| D | LYS460 |
| D | GLY463 |
| D | HOH697 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA D 503 |
| Chain | Residue |
| D | ILE29 |
| D | ASP97 |
| D | ILE184 |
| D | HOH832 |
| site_id | BC4 |
| Number of Residues | 36 |
| 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 | ASP218 |
| E | PHE231 |
| E | GLY233 |
| E | GLY234 |
| E | THR237 |
| E | HIS240 |
| E | ILE241 |
| E | GLU255 |
| E | GLY257 |
| E | CME289 |
| E | HIS336 |
| E | LYS339 |
| E | GLU390 |
| E | PHE392 |
| E | HOH628 |
| E | HOH678 |
| E | HOH728 |
| E | HOH770 |
| E | HOH792 |
| E | HOH806 |
| E | HOH933 |
| E | HOH965 |
| E | HOH1079 |
| E | HOH1214 |
| E | HOH1225 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NA E 502 |
| Chain | Residue |
| E | NA503 |
| E | HOH925 |
| E | HOH993 |
| F | HOH602 |
| F | HOH605 |
| F | HOH845 |
| F | HOH1032 |
| site_id | BC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NA E 503 |
| Chain | Residue |
| E | NA502 |
| E | HOH925 |
| E | HOH1050 |
| E | HOH1227 |
| F | HOH602 |
| F | HOH845 |
| F | HOH936 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA E 504 |
| Chain | Residue |
| E | LYS460 |
| E | GLY463 |
| E | HOH619 |
| F | VAL249 |
| F | HOH666 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA E 505 |
| Chain | Residue |
| E | ILE28 |
| E | ILE29 |
| E | ASP97 |
| E | ILE184 |
| E | HOH849 |
| site_id | BC9 |
| Number of Residues | 37 |
| Details | BINDING SITE FOR RESIDUE NAD F 501 |
| Chain | Residue |
| F | ILE153 |
| F | THR154 |
| F | PRO155 |
| F | TRP156 |
| F | ASN157 |
| F | GLN162 |
| F | LYS180 |
| F | SER182 |
| F | GLU183 |
| F | GLY213 |
| F | GLY217 |
| F | PHE231 |
| F | GLY233 |
| F | GLY234 |
| F | THR237 |
| F | HIS240 |
| F | ILE241 |
| F | GLU255 |
| F | GLY257 |
| F | CME289 |
| F | HIS336 |
| F | LYS339 |
| F | GLU390 |
| F | PHE392 |
| F | HOH616 |
| F | HOH671 |
| F | HOH692 |
| F | HOH708 |
| F | HOH729 |
| F | HOH780 |
| F | HOH809 |
| F | HOH859 |
| F | HOH976 |
| F | HOH1169 |
| F | HOH1200 |
| F | HOH1217 |
| F | HOH1235 |
| site_id | CC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA F 502 |
| Chain | Residue |
| C | SER342 |
| C | HOH661 |
| F | LEU7 |
| F | GLN9 |
| F | HOH765 |
| site_id | CC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA F 503 |
| Chain | Residue |
| F | ILE28 |
| F | ILE29 |
| F | ASP97 |
| F | ILE184 |
| F | HOH783 |
| site_id | CC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA F 504 |
| Chain | Residue |
| E | VAL249 |
| E | HOH635 |
| F | LYS460 |
| F | GLY463 |
| F | HOH670 |
| site_id | CC4 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAD G 501 |
| Chain | Residue |
| G | ILE153 |
| G | THR154 |
| G | PRO155 |
| G | TRP156 |
| G | ASN157 |
| G | LYS180 |
| G | PRO181 |
| G | SER182 |
| G | GLU183 |
| G | GLY213 |
| G | GLY217 |
| G | PHE231 |
| G | GLY233 |
| G | GLY234 |
| G | THR237 |
| G | HIS240 |
| G | GLU255 |
| G | GLY257 |
| G | CME289 |
| G | HIS336 |
| G | LYS339 |
| G | GLU390 |
| G | PHE392 |
| G | HOH692 |
| G | HOH701 |
| G | HOH845 |
| G | HOH957 |
| G | HOH983 |
| G | HOH987 |
| G | HOH991 |
| G | HOH1148 |
| G | HOH1152 |
| site_id | CC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA G 502 |
| Chain | Residue |
| G | LYS460 |
| G | GLY463 |
| G | HOH702 |
| H | VAL249 |
| H | HOH683 |
| site_id | CC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA G 503 |
| Chain | Residue |
| G | ILE29 |
| G | ASP97 |
| G | ILE184 |
| G | HOH1062 |
| site_id | CC7 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAD H 501 |
| Chain | Residue |
| H | ILE153 |
| H | THR154 |
| H | PRO155 |
| H | TRP156 |
| H | ASN157 |
| H | LYS180 |
| H | SER182 |
| H | GLU183 |
| H | GLY213 |
| H | GLY217 |
| H | PHE231 |
| H | GLY233 |
| H | GLY234 |
| H | THR237 |
| H | HIS240 |
| H | ILE241 |
| H | GLU255 |
| H | GLY257 |
| H | CME289 |
| H | HIS336 |
| H | LYS339 |
| H | GLU390 |
| H | PHE392 |
| H | HOH717 |
| H | HOH771 |
| H | HOH785 |
| H | HOH856 |
| H | HOH887 |
| H | HOH940 |
| H | HOH1054 |
| H | HOH1060 |
| H | HOH1186 |
| site_id | CC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA H 502 |
| Chain | Residue |
| G | VAL249 |
| G | HOH684 |
| H | LYS460 |
| H | GLY463 |
| H | HOH699 |
| site_id | CC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA H 503 |
| Chain | Residue |
| H | ILE29 |
| H | ASP97 |
| H | ILE184 |
| H | HOH947 |
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 |
