4Q92
1.90 Angstrom resolution crystal structure of apo betaine aldehyde dehydrogenase (betB) G234S mutant from Staphylococcus aureus (IDP00699) with BME-modified Cys289
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| A | 0046872 | molecular_function | metal ion 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 | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| B | 0046872 | molecular_function | metal ion 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 | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| C | 0046872 | molecular_function | metal ion 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 | 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 | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 501 |
| Chain | Residue |
| A | GLY286 |
| A | GLU390 |
| A | GLY393 |
| A | HOH644 |
| A | HOH785 |
| A | HOH956 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 502 |
| Chain | Residue |
| B | VAL249 |
| B | HOH912 |
| A | LYS460 |
| A | GLY463 |
| A | HOH690 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG A 503 |
| Chain | Residue |
| A | ARG77 |
| A | ASP81 |
| D | ASP81 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 501 |
| Chain | Residue |
| A | VAL249 |
| A | HOH978 |
| B | LYS460 |
| B | GLY463 |
| B | HOH699 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA C 501 |
| Chain | Residue |
| C | LYS460 |
| C | GLY463 |
| C | HOH646 |
| D | VAL249 |
| D | HOH645 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA C 502 |
| Chain | Residue |
| C | GLY286 |
| C | SER293 |
| C | GLY393 |
| C | HOH651 |
| C | HOH1001 |
| C | HOH1030 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PEG C 503 |
| Chain | Residue |
| B | ASP81 |
| C | ASP81 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA D 501 |
| Chain | Residue |
| C | VAL249 |
| C | HOH662 |
| D | LYS460 |
| D | GLY463 |
| D | HOH608 |
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 |
