5A2D
CRYSTAL STRUCTURE OF BETAINE ALDEHYDE DEHYDROGENASE FROM SPINACH SHOWING A THIOHEMIACETAL WITH BETAINE ALDEHYDE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006081 | biological_process | cellular aldehyde metabolic process |
| 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 | 0019145 | molecular_function | aminobutyraldehyde dehydrogenase activity |
| A | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| A | 0030955 | molecular_function | potassium ion binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047105 | molecular_function | 4-trimethylammoniobutyraldehyde dehydrogenase activity |
| A | 0110095 | biological_process | cellular detoxification of aldehyde |
| B | 0006081 | biological_process | cellular aldehyde metabolic process |
| 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 | 0019145 | molecular_function | aminobutyraldehyde dehydrogenase activity |
| B | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| B | 0030955 | molecular_function | potassium ion binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047105 | molecular_function | 4-trimethylammoniobutyraldehyde dehydrogenase activity |
| B | 0110095 | biological_process | cellular detoxification of aldehyde |
| C | 0006081 | biological_process | cellular aldehyde metabolic process |
| 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 | 0019145 | molecular_function | aminobutyraldehyde dehydrogenase activity |
| C | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| C | 0030955 | molecular_function | potassium ion binding |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0047105 | molecular_function | 4-trimethylammoniobutyraldehyde dehydrogenase activity |
| C | 0110095 | biological_process | cellular detoxification of aldehyde |
| D | 0006081 | biological_process | cellular aldehyde metabolic process |
| 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 | 0019145 | molecular_function | aminobutyraldehyde dehydrogenase activity |
| D | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| D | 0030955 | molecular_function | potassium ion binding |
| D | 0042803 | molecular_function | protein homodimerization activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0047105 | molecular_function | 4-trimethylammoniobutyraldehyde dehydrogenase activity |
| D | 0110095 | biological_process | cellular detoxification of aldehyde |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CHT A 1497 |
| Chain | Residue |
| A | TYR160 |
| A | ILE290 |
| A | CYS291 |
| A | SER292 |
| A | GLN448 |
| A | CYS450 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CHT B 1497 |
| Chain | Residue |
| B | ILE290 |
| B | SER292 |
| B | GLN448 |
| B | CYS450 |
| B | TYR160 |
| B | MET164 |
| B | TRP167 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ETX D 1498 |
| Chain | Residue |
| D | PRO157 |
| D | ASN159 |
| D | THR234 |
| D | GLY235 |
| D | SER236 |
| D | GLY259 |
| D | CSO291 |
| D | GLU390 |
| D | PHE392 |
| D | HOH2179 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ETX A 1498 |
| Chain | Residue |
| A | GLU415 |
| A | TYR416 |
| A | ARG461 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PG4 B 1498 |
| Chain | Residue |
| A | TRP471 |
| A | GLN474 |
| B | GLU470 |
| B | TRP471 |
| B | GLN474 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE AE3 C 1497 |
| Chain | Residue |
| C | GLN474 |
| D | GLU470 |
| D | TRP471 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K A 1499 |
| Chain | Residue |
| A | ILE28 |
| A | ASP96 |
| A | LEU186 |
| A | HOH2022 |
| A | HOH2023 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K B 1499 |
| Chain | Residue |
| B | ILE28 |
| B | ASP96 |
| B | LEU186 |
| B | HOH2015 |
| B | HOH2018 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K C 1498 |
| Chain | Residue |
| C | VAL27 |
| C | ILE28 |
| C | ASP96 |
| C | LEU186 |
| C | HOH2037 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K D 1499 |
| Chain | Residue |
| D | ILE28 |
| D | ASP96 |
| D | LEU186 |
| D | HOH2019 |
| D | HOH2088 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL D 1500 |
| Chain | Residue |
| C | LYS460 |
| D | ARG55 |
| D | PRO226 |
| D | ASP227 |
| D | ASP229 |
| D | HOH2027 |
Functional Information from PROSITE/UniProt
| site_id | PS00070 |
| Number of Residues | 12 |
| Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FwTNGQICSATS |
| Chain | Residue | Details |
| D | PHE284-SER295 | |
| A | PHE284-SER295 | |
| C | PHE284-SER295 |
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKSP |
| Chain | Residue | Details |
| D | LEU256-PRO263 | |
| A | LEU256-PRO263 | |
| C | LEU256-PRO263 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000255|PROSITE-ProRule:PRU10008 |
| Chain | Residue | Details |
| D | GLU257 | |
| B | GLU257 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000255|PROSITE-ProRule:PRU10008, ECO:0000305|PubMed:22345508 |
| Chain | Residue | Details |
| D | CSO291 | |
| B | CYS291 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22345508, ECO:0000269|PubMed:26792760, ECO:0007744|PDB:4A0M, ECO:0007744|PDB:5A2D |
| Chain | Residue | Details |
| D | LEU186 | |
| D | LYS460 | |
| B | ILE28 | |
| B | ASP96 | |
| B | LEU186 | |
| B | LYS460 | |
| D | ILE28 | |
| D | ASP96 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22345508, ECO:0007744|PDB:4A0M, ECO:0007744|PDB:4V37 |
| Chain | Residue | Details |
| D | TRP456 | |
| B | SER156 | |
| B | LYS182 | |
| B | SER236 | |
| B | GLU390 | |
| B | TRP456 | |
| D | SER236 | |
| D | GLU390 | |
| D | SER156 | |
| D | LYS182 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | BINDING: in other chain => ECO:0000269|PubMed:22345508, ECO:0000269|PubMed:26792760, ECO:0007744|PDB:4A0M, ECO:0007744|PDB:5A2D |
| Chain | Residue | Details |
| D | VAL251 | |
| B | VAL251 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22345508, ECO:0007744|PDB:4V37 |
| Chain | Residue | Details |
| D | LEU258 | |
| B | LEU258 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P20000 |
| Chain | Residue | Details |
| D | ASN159 | |
| B | ASN159 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | MOD_RES: Blocked amino end (Arg) |
| Chain | Residue | Details |
| D | ARG8 | |
| B | ARG8 |
