4V37
Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 0019145 | molecular_function | aminobutyraldehyde dehydrogenase (NAD+) 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 | 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 | 0019145 | molecular_function | aminobutyraldehyde dehydrogenase (NAD+) 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 | 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 | 0019145 | molecular_function | aminobutyraldehyde dehydrogenase (NAD+) 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 | 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 | 0019145 | molecular_function | aminobutyraldehyde dehydrogenase (NAD+) 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 | 30 |
| Details | BINDING SITE FOR RESIDUE NAD B 1498 |
| Chain | Residue |
| B | ILE155 |
| B | GLU185 |
| B | GLY215 |
| B | GLY219 |
| B | ALA220 |
| B | PHE233 |
| B | THR234 |
| B | GLY235 |
| B | SER236 |
| B | THR239 |
| B | GLU257 |
| B | SER156 |
| B | LEU258 |
| B | GLY259 |
| B | ALA291 |
| B | GLU390 |
| B | PHE392 |
| B | TRP456 |
| B | FMT1500 |
| B | HOH2274 |
| B | HOH2276 |
| B | HOH2277 |
| B | PRO157 |
| B | HOH2278 |
| B | TRP158 |
| B | ASN159 |
| B | MET164 |
| B | LYS182 |
| B | PRO183 |
| B | SER184 |
| site_id | AC2 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAD A 1498 |
| Chain | Residue |
| A | ILE155 |
| A | SER156 |
| A | PRO157 |
| A | TRP158 |
| A | ASN159 |
| A | MET164 |
| A | LYS182 |
| A | PRO183 |
| A | SER184 |
| A | GLU185 |
| A | GLY215 |
| A | GLY219 |
| A | ALA220 |
| A | PHE233 |
| A | THR234 |
| A | GLY235 |
| A | SER236 |
| A | THR239 |
| A | GLU257 |
| A | LEU258 |
| A | GLY259 |
| A | ALA291 |
| A | GLU390 |
| A | PHE392 |
| A | TRP456 |
| A | FMT1500 |
| A | HOH2183 |
| A | HOH2207 |
| A | HOH2211 |
| A | HOH2258 |
| A | HOH2337 |
| A | HOH2338 |
| site_id | AC3 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAD D 1497 |
| Chain | Residue |
| D | ILE155 |
| D | SER156 |
| D | PRO157 |
| D | TRP158 |
| D | ASN159 |
| D | LYS182 |
| D | PRO183 |
| D | SER184 |
| D | GLU185 |
| D | GLY215 |
| D | GLY219 |
| D | ALA220 |
| D | PHE233 |
| D | THR234 |
| D | GLY235 |
| D | SER236 |
| D | THR239 |
| D | GLU257 |
| D | LEU258 |
| D | GLY259 |
| D | ALA291 |
| D | GLU390 |
| D | PHE392 |
| D | TRP456 |
| D | FMT1499 |
| D | HOH2121 |
| D | HOH2128 |
| D | HOH2132 |
| D | HOH2153 |
| D | HOH2251 |
| D | HOH2252 |
| D | HOH2254 |
| D | HOH2256 |
| site_id | AC4 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAD C 1498 |
| Chain | Residue |
| C | ASN159 |
| C | LYS182 |
| C | PRO183 |
| C | SER184 |
| C | GLU185 |
| C | GLY215 |
| C | GLY219 |
| C | ALA220 |
| C | PHE233 |
| C | THR234 |
| C | GLY235 |
| C | SER236 |
| C | THR239 |
| C | GLU257 |
| C | LEU258 |
| C | GLY259 |
| C | ALA291 |
| C | GLU390 |
| C | PHE392 |
| C | TRP456 |
| C | FMT1501 |
| C | HOH2148 |
| C | HOH2149 |
| C | HOH2179 |
| C | HOH2299 |
| C | HOH2300 |
| C | HOH2301 |
| C | ILE155 |
| C | SER156 |
| C | PRO157 |
| C | TRP158 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE 0D8 A 1499 |
| Chain | Residue |
| A | TRP167 |
| A | SER292 |
| A | CYS450 |
| A | TRP456 |
| A | FMT1500 |
| A | HOH2235 |
| A | HOH2302 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE 0D8 B 1499 |
| Chain | Residue |
| A | HOH2321 |
| B | SER292 |
| B | CYS450 |
| B | TRP456 |
| B | FMT1500 |
| B | HOH2185 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE 0D8 C 1499 |
| Chain | Residue |
| C | TRP167 |
| C | SER292 |
| C | CYS450 |
| C | TRP456 |
| C | FMT1501 |
| C | HOH2263 |
| C | HOH2265 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE 0D8 D 1498 |
| Chain | Residue |
| C | HOH2286 |
| D | SER292 |
| D | CYS450 |
| D | TRP456 |
| D | FMT1499 |
| D | HOH2176 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE 0D8 C 1500 |
| Chain | Residue |
| C | TRP285 |
| C | GLN448 |
| C | PRO449 |
| C | CYS450 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FMT D 1499 |
| Chain | Residue |
| D | ASN159 |
| D | TYR160 |
| D | ILE290 |
| D | ALA291 |
| D | SER292 |
| D | NAD1497 |
| D | 0D81498 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FMT C 1501 |
| Chain | Residue |
| C | ASN159 |
| C | TYR160 |
| C | ILE290 |
| C | ALA291 |
| C | SER292 |
| C | NAD1498 |
| C | 0D81499 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FMT A 1500 |
| Chain | Residue |
| A | ASN159 |
| A | TYR160 |
| A | ILE290 |
| A | ALA291 |
| A | SER292 |
| A | NAD1498 |
| A | 0D81499 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT B 1500 |
| Chain | Residue |
| B | ASN159 |
| B | TYR160 |
| B | ALA291 |
| B | SER292 |
| B | NAD1498 |
| B | 0D81499 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PG4 A 1501 |
| Chain | Residue |
| A | ARG146 |
| A | GLU470 |
| A | TRP471 |
| A | GLN474 |
| A | HOH2339 |
| B | TRP471 |
| B | GLN474 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PG4 C 1502 |
| Chain | Residue |
| C | TRP471 |
| C | GLN474 |
| C | HOH2304 |
| D | TRP471 |
| D | GLN474 |
| site_id | BC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE AE3 B 1501 |
| Chain | Residue |
| B | TRP285 |
| B | GLN448 |
| B | PRO449 |
| B | CYS450 |
| B | HOH2087 |
| B | HOH2091 |
| B | HOH2092 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K A 1502 |
| Chain | Residue |
| A | ILE28 |
| A | ASP96 |
| A | LEU186 |
| A | HOH2043 |
| A | HOH2044 |
| site_id | BC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K B 1502 |
| Chain | Residue |
| B | ILE28 |
| B | ASP96 |
| B | LEU186 |
| B | HOH2030 |
| B | HOH2138 |
| site_id | CC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE K C 1503 |
| Chain | Residue |
| C | ILE28 |
| C | ASP96 |
| C | LEU186 |
| C | HOH2027 |
| site_id | CC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K D 1500 |
| Chain | Residue |
| D | ILE28 |
| D | ASP96 |
| D | LEU186 |
| D | HOH2034 |
| D | HOH2133 |
Functional Information from PROSITE/UniProt
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKSP |
| Chain | Residue | Details |
| A | LEU256-PRO263 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000255|PROSITE-ProRule:PRU10008 |
| Chain | Residue | Details |
| A | GLU257 | |
| B | GLU257 | |
| C | GLU257 | |
| D | GLU257 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000255|PROSITE-ProRule:PRU10008, ECO:0000305|PubMed:22345508 |
| Chain | Residue | Details |
| A | ALA291 | |
| B | ALA291 | |
| C | ALA291 | |
| D | ALA291 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22345508, ECO:0000269|PubMed:26792760, ECO:0007744|PDB:4A0M, ECO:0007744|PDB:5A2D |
| Chain | Residue | Details |
| A | ILE28 | |
| C | ASP96 | |
| C | LEU186 | |
| C | LYS460 | |
| D | ILE28 | |
| D | ASP96 | |
| D | LEU186 | |
| D | LYS460 | |
| A | ASP96 | |
| A | LEU186 | |
| A | LYS460 | |
| B | ILE28 | |
| B | ASP96 | |
| B | LEU186 | |
| B | LYS460 | |
| C | ILE28 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22345508, ECO:0007744|PDB:4A0M, ECO:0007744|PDB:4V37 |
| Chain | Residue | Details |
| A | SER156 | |
| B | TRP456 | |
| C | SER156 | |
| C | LYS182 | |
| C | SER236 | |
| C | GLU390 | |
| C | TRP456 | |
| D | SER156 | |
| D | LYS182 | |
| D | SER236 | |
| D | GLU390 | |
| A | LYS182 | |
| D | TRP456 | |
| A | SER236 | |
| A | GLU390 | |
| A | TRP456 | |
| B | SER156 | |
| B | LYS182 | |
| B | SER236 | |
| B | GLU390 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | BINDING: in other chain => ECO:0000269|PubMed:22345508, ECO:0000269|PubMed:26792760, ECO:0007744|PDB:4A0M, ECO:0007744|PDB:5A2D |
| Chain | Residue | Details |
| A | VAL251 | |
| B | VAL251 | |
| C | VAL251 | |
| D | VAL251 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22345508, ECO:0007744|PDB:4V37 |
| Chain | Residue | Details |
| A | LEU258 | |
| B | LEU258 | |
| C | LEU258 | |
| D | LEU258 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P20000 |
| Chain | Residue | Details |
| A | ASN159 | |
| B | ASN159 | |
| C | ASN159 | |
| D | ASN159 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | MOD_RES: Blocked amino end (Arg) |
| Chain | Residue | Details |
| A | ARG8 | |
| B | ARG8 | |
| C | ARG8 | |
| D | ARG8 |
