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 |