4QTO
1.65 Angstrom resolution crystal structure of betaine aldehyde dehydrogenase (betB) from Staphylococcus aureus with BME-modified Cys289 and PEG molecule in active site
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 |
| 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 |
| 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 |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 501 |
| Chain | Residue |
| A | LYS460 |
| A | GLY463 |
| A | HOH652 |
| B | VAL249 |
| B | HOH613 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PGE A 502 |
| Chain | Residue |
| A | HOH1263 |
| A | HOH1274 |
| A | PHE283 |
| A | HIS448 |
| A | TYR450 |
| A | HOH1108 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PGE A 503 |
| Chain | Residue |
| A | SER342 |
| A | TYR343 |
| A | VAL346 |
| A | ARG385 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PEG A 504 |
| Chain | Residue |
| A | SER8 |
| A | TRP17 |
| A | GLU197 |
| A | HOH1235 |
| A | HOH1264 |
| B | ASP267 |
| B | ALA268 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PEG A 505 |
| Chain | Residue |
| A | PRO155 |
| A | GLY234 |
| A | CME289 |
| A | HIS336 |
| A | PHE392 |
| A | HOH830 |
| A | HOH954 |
| A | HOH988 |
| A | HOH1022 |
| A | HOH1119 |
| A | HOH1260 |
| A | HOH1261 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG A 506 |
| Chain | Residue |
| A | SER61 |
| A | GLY62 |
| A | GLU63 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE TRS A 507 |
| Chain | Residue |
| A | GLU103 |
| A | ALA324 |
| A | THR326 |
| A | GLU327 |
| A | HOH809 |
| B | TRP493 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 501 |
| Chain | Residue |
| A | VAL249 |
| A | HOH621 |
| B | LYS460 |
| B | GLY463 |
| B | HOH663 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PGE B 502 |
| Chain | Residue |
| B | ALA107 |
| B | TYR158 |
| B | HIS448 |
| B | TYR450 |
| B | HOH1191 |
| B | HOH1239 |
| B | HOH1241 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG B 503 |
| Chain | Residue |
| B | GLN66 |
| B | GLU67 |
| B | HOH1092 |
| site_id | BC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PEG B 504 |
| Chain | Residue |
| B | CME289 |
| B | HIS336 |
| B | LYS339 |
| B | PHE392 |
| B | HOH906 |
| B | HOH937 |
| B | HOH996 |
| B | HOH1003 |
| B | HOH1225 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE TRS B 505 |
| Chain | Residue |
| A | TRP493 |
| B | GLU103 |
| B | ALA324 |
| B | THR326 |
| B | HOH1178 |
| B | HOH1236 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA C 501 |
| Chain | Residue |
| C | LYS460 |
| C | GLY463 |
| C | HOH661 |
| D | VAL249 |
| D | HOH665 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PGE C 502 |
| Chain | Residue |
| C | TYR158 |
| C | PHE283 |
| C | HIS448 |
| C | TYR450 |
| C | HOH1052 |
| D | TRP493 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PG4 C 503 |
| Chain | Residue |
| C | SER342 |
| C | TYR343 |
| C | VAL346 |
| C | ARG385 |
| C | HOH904 |
| C | HOH967 |
| site_id | BC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE EDO C 504 |
| Chain | Residue |
| C | HOH1261 |
| C | PRO155 |
| C | GLY233 |
| C | GLY234 |
| C | CME289 |
| C | PHE392 |
| C | HOH803 |
| C | HOH951 |
| C | HOH1241 |
| C | HOH1260 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA D 501 |
| Chain | Residue |
| C | VAL249 |
| C | HOH699 |
| D | LYS460 |
| D | GLY463 |
| D | HOH697 |
| site_id | BC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PGE D 502 |
| Chain | Residue |
| D | TYR158 |
| D | HIS448 |
| D | TYR450 |
| D | HOH1007 |
| D | HOH1085 |
| D | HOH1271 |
| D | HOH1276 |
| site_id | CC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG D 503 |
| Chain | Residue |
| D | SER61 |
| D | GLY62 |
| D | GLU63 |
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 |
