4QJE
1.85 Angstrom resolution crystal structure of apo betaine aldehyde dehydrogenase (betB) G234S mutant from Staphylococcus aureus (IDP00699) with BME-free sulfinic acid form of Cys289
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
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 | 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 | 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 | 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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NA A 501 |
Chain | Residue |
A | ILE29 |
A | ASP97 |
A | ILE184 |
A | HOH856 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA A 502 |
Chain | Residue |
A | LYS460 |
A | GLY463 |
A | HOH612 |
B | VAL249 |
B | HOH728 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PEG A 503 |
Chain | Residue |
A | SER61 |
A | GLY62 |
A | GLU63 |
A | GLN66 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PEG A 504 |
Chain | Residue |
A | SER342 |
A | TYR343 |
A | VAL346 |
A | ARG385 |
A | HOH1016 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE TRS A 505 |
Chain | Residue |
A | GLU103 |
A | ALA324 |
A | THR326 |
A | HOH655 |
A | HOH1095 |
A | HOH1152 |
B | TRP493 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NA B 501 |
Chain | Residue |
B | ILE29 |
B | ASP97 |
B | ILE184 |
B | HOH777 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA B 502 |
Chain | Residue |
A | VAL249 |
A | HOH657 |
B | LYS460 |
B | GLY463 |
B | HOH621 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PEG B 503 |
Chain | Residue |
B | GLY62 |
B | GLU63 |
B | GLN66 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NA C 501 |
Chain | Residue |
C | ILE29 |
C | ASP97 |
C | ILE184 |
C | HOH763 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA C 502 |
Chain | Residue |
C | LYS460 |
C | GLY463 |
C | HOH618 |
D | VAL249 |
D | HOH662 |
site_id | BC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE PEG C 503 |
Chain | Residue |
C | ASN487 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PEG C 504 |
Chain | Residue |
C | SER342 |
C | TYR343 |
C | VAL346 |
C | ARG385 |
C | HOH1023 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PEG C 505 |
Chain | Residue |
C | GLY62 |
C | GLU63 |
C | GLU67 |
C | HOH969 |
site_id | BC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE TRS C 506 |
Chain | Residue |
C | TRP493 |
C | HOH643 |
C | HOH972 |
C | HOH1140 |
D | GLU103 |
D | ALA324 |
D | THR326 |
site_id | BC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE TRS C 507 |
Chain | Residue |
C | GLU103 |
C | ALA324 |
C | THR326 |
C | HOH725 |
C | HOH1029 |
C | HOH1080 |
D | TRP493 |
site_id | BC7 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE B3P C 508 |
Chain | Residue |
C | TRP17 |
C | ARG191 |
C | GLU194 |
C | GLU197 |
C | GLU198 |
C | HOH663 |
C | HOH839 |
C | HOH895 |
C | HOH1150 |
C | HOH1185 |
C | HOH1221 |
site_id | BC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NA D 501 |
Chain | Residue |
D | ILE29 |
D | ASP97 |
D | ILE184 |
D | HOH800 |
site_id | BC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA D 502 |
Chain | Residue |
C | VAL249 |
C | HOH657 |
D | LYS460 |
D | GLY463 |
D | HOH632 |
site_id | CC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PEG D 503 |
Chain | Residue |
D | GLY62 |
D | GLU63 |
D | GLN66 |
D | HOH1073 |
D | HOH1204 |
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 |
B | TYR282-SER293 | |
A | TYR282-SER293 |
site_id | PS00687 |
Number of Residues | 8 |
Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKNP |
Chain | Residue | Details |
B | LEU254-PRO261 | |
A | LEU254-PRO261 |