4MPB
1.7 Angstrom resolution crystal structure of betaine aldehyde dehydrogenase (betB) from Staphylococcus aureus
Replaces: 3ED6Functional 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG A 501 |
| Chain | Residue |
| A | VAL249 |
| A | LYS460 |
| A | HOH679 |
| A | HOH693 |
| A | HOH709 |
| A | HOH842 |
| A | HOH1012 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 502 |
| Chain | Residue |
| A | HOH1016 |
| A | HOH1017 |
| A | HOH1018 |
| A | HOH916 |
| A | HOH1015 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 503 |
| Chain | Residue |
| A | HOH1023 |
| A | HOH1024 |
| A | HOH1025 |
| A | HOH1026 |
| A | HOH1203 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 504 |
| Chain | Residue |
| A | GLN298 |
| A | LYS429 |
| A | HOH833 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG B 501 |
| Chain | Residue |
| B | VAL249 |
| B | LYS460 |
| B | HOH1085 |
| B | HOH1109 |
| B | HOH1144 |
| B | HOH1195 |
| B | HOH1435 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 502 |
| Chain | Residue |
| B | HOH1190 |
| B | HOH1212 |
| B | HOH1306 |
| B | HOH1440 |
| B | HOH1441 |
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 |
