6QAP
Structure of the human aldehyde dehydrogenase 9A1 in C2 space group
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005829 | cellular_component | cytosol |
| A | 0006081 | biological_process | cellular aldehyde metabolic process |
| 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 | 0018467 | molecular_function | formaldehyde dehydrogenase (NAD+) activity |
| A | 0019145 | molecular_function | aminobutyraldehyde dehydrogenase (NAD+) activity |
| A | 0036094 | molecular_function | small molecule binding |
| A | 0045329 | biological_process | carnitine biosynthetic process |
| A | 0047105 | molecular_function | 4-trimethylammoniobutyraldehyde dehydrogenase activity |
| A | 0051289 | biological_process | protein homotetramerization |
| A | 0070062 | cellular_component | extracellular exosome |
| B | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005829 | cellular_component | cytosol |
| B | 0006081 | biological_process | cellular aldehyde metabolic process |
| 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 | 0018467 | molecular_function | formaldehyde dehydrogenase (NAD+) activity |
| B | 0019145 | molecular_function | aminobutyraldehyde dehydrogenase (NAD+) activity |
| B | 0036094 | molecular_function | small molecule binding |
| B | 0045329 | biological_process | carnitine biosynthetic process |
| B | 0047105 | molecular_function | 4-trimethylammoniobutyraldehyde dehydrogenase activity |
| B | 0051289 | biological_process | protein homotetramerization |
| B | 0070062 | cellular_component | extracellular exosome |
| C | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005739 | cellular_component | mitochondrion |
| C | 0005829 | cellular_component | cytosol |
| C | 0006081 | biological_process | cellular aldehyde metabolic process |
| 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 | 0018467 | molecular_function | formaldehyde dehydrogenase (NAD+) activity |
| C | 0019145 | molecular_function | aminobutyraldehyde dehydrogenase (NAD+) activity |
| C | 0036094 | molecular_function | small molecule binding |
| C | 0045329 | biological_process | carnitine biosynthetic process |
| C | 0047105 | molecular_function | 4-trimethylammoniobutyraldehyde dehydrogenase activity |
| C | 0051289 | biological_process | protein homotetramerization |
| C | 0070062 | cellular_component | extracellular exosome |
| D | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005739 | cellular_component | mitochondrion |
| D | 0005829 | cellular_component | cytosol |
| D | 0006081 | biological_process | cellular aldehyde metabolic process |
| 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 | 0018467 | molecular_function | formaldehyde dehydrogenase (NAD+) activity |
| D | 0019145 | molecular_function | aminobutyraldehyde dehydrogenase (NAD+) activity |
| D | 0036094 | molecular_function | small molecule binding |
| D | 0045329 | biological_process | carnitine biosynthetic process |
| D | 0047105 | molecular_function | 4-trimethylammoniobutyraldehyde dehydrogenase activity |
| D | 0051289 | biological_process | protein homotetramerization |
| D | 0070062 | cellular_component | extracellular exosome |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 1 |
| Details | binding site for residue EDO A 501 |
| Chain | Residue |
| A | SER229 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 502 |
| Chain | Residue |
| A | LYS227 |
| A | VAL228 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 503 |
| Chain | Residue |
| A | THR44 |
| A | GLN210 |
| A | PRO11 |
| A | LEU12 |
| A | ASN13 |
| A | GLU21 |
| A | PRO22 |
| A | PHE43 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 504 |
| Chain | Residue |
| A | GLU118 |
| A | TYR119 |
| A | HOH610 |
| D | CYS74 |
| D | GLY122 |
| D | HOH617 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 505 |
| Chain | Residue |
| A | GLY154 |
| A | ALA155 |
| A | PRO159 |
| A | PHE179 |
| A | PRO181 |
| A | SER182 |
| A | THR185 |
| A | HOH603 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 501 |
| Chain | Residue |
| B | GLU118 |
| B | TYR119 |
| B | GLY122 |
| C | GLY122 |
| C | PEG506 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 502 |
| Chain | Residue |
| B | ARG467 |
| B | ARG471 |
| B | HOH636 |
| C | ARG467 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | binding site for residue EDO B 503 |
| Chain | Residue |
| B | SER229 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue PEG B 504 |
| Chain | Residue |
| B | ASP24 |
| B | ALA25 |
| B | LYS49 |
| C | THR28 |
| C | GLU29 |
| site_id | AD1 |
| Number of Residues | 1 |
| Details | binding site for residue NA C 501 |
| Chain | Residue |
| C | HOH677 |
| site_id | AD2 |
| Number of Residues | 2 |
| Details | binding site for residue NA C 502 |
| Chain | Residue |
| C | GLN10 |
| C | GLU194 |
| site_id | AD3 |
| Number of Residues | 2 |
| Details | binding site for residue NA C 503 |
| Chain | Residue |
| C | SER9 |
| C | GLN10 |
| site_id | AD4 |
| Number of Residues | 1 |
| Details | binding site for residue EDO C 504 |
| Chain | Residue |
| C | SER9 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue PEG C 505 |
| Chain | Residue |
| C | SER229 |
| C | VAL472 |
| C | THR473 |
| C | TYR476 |
| site_id | AD6 |
| Number of Residues | 7 |
| Details | binding site for residue PEG C 506 |
| Chain | Residue |
| B | MET71 |
| B | CYS74 |
| B | GLY122 |
| B | EDO501 |
| B | HOH610 |
| C | GLN115 |
| C | GLU118 |
| site_id | AD7 |
| Number of Residues | 8 |
| Details | binding site for residue PEG C 507 |
| Chain | Residue |
| C | ILE153 |
| C | GLY154 |
| C | LYS180 |
| C | SER182 |
| C | PRO183 |
| C | GLY212 |
| C | ALA213 |
| C | HOH621 |
| site_id | AD8 |
| Number of Residues | 8 |
| Details | binding site for residue NA D 501 |
| Chain | Residue |
| D | TYR14 |
| D | ARG15 |
| D | GLY16 |
| D | GLY17 |
| D | GLY204 |
| D | PHE206 |
| D | ASN207 |
| D | EDO507 |
| site_id | AD9 |
| Number of Residues | 2 |
| Details | binding site for residue NA D 502 |
| Chain | Residue |
| D | GLU118 |
| D | EDO506 |
| site_id | AE1 |
| Number of Residues | 4 |
| Details | binding site for residue NA D 503 |
| Chain | Residue |
| D | ALA155 |
| D | PRO181 |
| D | SER182 |
| D | THR185 |
| site_id | AE2 |
| Number of Residues | 2 |
| Details | binding site for residue NA D 504 |
| Chain | Residue |
| D | SER9 |
| D | GLN10 |
| site_id | AE3 |
| Number of Residues | 2 |
| Details | binding site for residue NA D 505 |
| Chain | Residue |
| D | GLN10 |
| D | GLU194 |
| site_id | AE4 |
| Number of Residues | 5 |
| Details | binding site for residue EDO D 506 |
| Chain | Residue |
| A | GLY122 |
| D | GLU118 |
| D | TYR119 |
| D | GLY122 |
| D | NA502 |
| site_id | AE5 |
| Number of Residues | 10 |
| Details | binding site for residue EDO D 507 |
| Chain | Residue |
| D | GLY17 |
| D | SER197 |
| D | VAL201 |
| D | PRO202 |
| D | PRO203 |
| D | GLY204 |
| D | LEU205 |
| D | PHE206 |
| D | NA501 |
| D | HOH603 |
| site_id | AE6 |
| Number of Residues | 7 |
| Details | binding site for residue EDO D 508 |
| Chain | Residue |
| D | ASN13 |
| D | GLU21 |
| D | PRO22 |
| D | PHE43 |
| D | THR44 |
| D | GLN210 |
| D | LEU12 |
| site_id | AE7 |
| Number of Residues | 2 |
| Details | binding site for residue EDO D 509 |
| Chain | Residue |
| D | GLU198 |
| D | GLY200 |
| site_id | AE8 |
| Number of Residues | 3 |
| Details | binding site for residue EDO D 510 |
| Chain | Residue |
| D | PHE104 |
| D | ARG107 |
| D | LEU108 |
| site_id | AE9 |
| Number of Residues | 4 |
| Details | binding site for residue EDO D 511 |
| Chain | Residue |
| C | GLU468 |
| D | ALA128 |
| D | GLY129 |
| D | ARG144 |
Functional Information from PROSITE/UniProt
| site_id | PS00070 |
| Number of Residues | 12 |
| Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FlTQGQVCCNGT |
| Chain | Residue | Details |
| A | PHE281-THR292 |
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKSP |
| Chain | Residue | Details |
| A | LEU253-PRO260 |
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 | GLU254 | |
| B | GLU254 | |
| C | GLU254 | |
| D | GLU254 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000255|PROSITE-ProRule:PRU10008 |
| Chain | Residue | Details |
| A | CYS288 | |
| B | CYS288 | |
| C | CYS288 | |
| D | CYS288 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P56533 |
| Chain | Residue | Details |
| A | LYS180 | |
| D | LYS180 | |
| D | GLY232 | |
| D | GLU391 | |
| A | GLY232 | |
| A | GLU391 | |
| B | LYS180 | |
| B | GLY232 | |
| B | GLU391 | |
| C | LYS180 | |
| C | GLY232 | |
| C | GLU391 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | SITE: Transition state stabilizer => ECO:0000250 |
| Chain | Residue | Details |
| A | ASN157 | |
| B | ASN157 | |
| C | ASN157 | |
| D | ASN157 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | MOD_RES: N-acetylserine; in 4-trimethylaminobutyraldehyde dehydrogenase, N-terminally processed => ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378 |
| Chain | Residue | Details |
| A | SER2 | |
| B | SER2 | |
| C | SER2 | |
| D | SER2 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9JLJ2 |
| Chain | Residue | Details |
| A | LYS30 | |
| A | LYS303 | |
| B | LYS30 | |
| B | LYS303 | |
| C | LYS30 | |
| C | LYS303 | |
| D | LYS30 | |
| D | LYS303 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9JLJ2 |
| Chain | Residue | Details |
| A | LYS59 | |
| B | LYS59 | |
| C | LYS59 | |
| D | LYS59 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | LYS298 | |
| B | LYS298 | |
| C | LYS298 | |
| D | LYS298 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9JLJ2 |
| Chain | Residue | Details |
| A | LYS344 | |
| B | LYS344 | |
| C | LYS344 | |
| D | LYS344 |
