5AC2
human aldehyde dehydrogenase 1A1 with duocarmycin analog
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0001523 | biological_process | retinoid metabolic process |
| A | 0001758 | molecular_function | retinal dehydrogenase activity |
| A | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
| A | 0005096 | molecular_function | GTPase activator activity |
| A | 0005497 | molecular_function | androgen binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006081 | biological_process | cellular aldehyde metabolic process |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0009449 | biological_process | gamma-aminobutyric acid biosynthetic 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 | 0018479 | molecular_function | benzaldehyde dehydrogenase (NAD+) activity |
| A | 0019145 | molecular_function | aminobutyraldehyde dehydrogenase (NAD+) activity |
| A | 0030392 | biological_process | fructosamine catabolic process |
| A | 0030424 | cellular_component | axon |
| A | 0036438 | biological_process | maintenance of lens transparency |
| A | 0042572 | biological_process | retinol metabolic process |
| A | 0042995 | cellular_component | cell projection |
| A | 0043878 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity |
| A | 0045202 | cellular_component | synapse |
| A | 0051287 | molecular_function | NAD binding |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0106373 | molecular_function | 3-deoxyglucosone dehydrogenase activity |
| A | 0110095 | biological_process | cellular detoxification of aldehyde |
| A | 0120163 | biological_process | negative regulation of cold-induced thermogenesis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE K9P A 1502 |
| Chain | Residue |
| A | PHE171 |
| A | TYR457 |
| A | GLY458 |
| A | MET175 |
| A | TRP178 |
| A | PHE290 |
| A | HIS293 |
| A | GLY294 |
| A | TYR297 |
| A | CYS302 |
| A | ILE304 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE YB A 1503 |
| Chain | Residue |
| A | ASP283 |
| site_id | AC3 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE TXE A 1504 |
| Chain | Residue |
| A | ILE166 |
| A | ILE167 |
| A | PRO168 |
| A | TRP169 |
| A | ASN170 |
| A | LYS193 |
| A | ALA195 |
| A | GLU196 |
| A | GLY226 |
| A | GLY230 |
| A | ALA231 |
| A | PHE244 |
| A | THR245 |
| A | GLY246 |
| A | SER247 |
| A | VAL250 |
| A | GLU269 |
| A | GLY271 |
| A | CYS303 |
| A | GLU349 |
| A | GLN350 |
| A | LYS353 |
| A | GLU400 |
| A | PHE402 |
| A | YB1508 |
| A | HOH2085 |
| A | HOH2089 |
| A | HOH2122 |
| A | HOH2123 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE YB A 1507 |
| Chain | Residue |
| A | HOH2016 |
| A | HOH2017 |
| A | HOH2018 |
| A | HOH2124 |
| A | HOH2130 |
| A | HOH2164 |
| A | HOH2164 |
| A | HOH2165 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE YB A 1508 |
| Chain | Residue |
| A | TXE1504 |
| A | HOH2089 |
| A | HOH2091 |
| A | HOH2122 |
| A | HOH2123 |
| A | HOH2163 |
| A | HOH2166 |
| A | HOH2167 |
Functional Information from PROSITE/UniProt
| site_id | PS00070 |
| Number of Residues | 12 |
| Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FyHQGQCCIAAS |
| Chain | Residue | Details |
| A | PHE296-SER307 |
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKSP |
| Chain | Residue | Details |
| A | LEU268-PRO275 |
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, ECO:0000269|PubMed:3676276 |
| Chain | Residue | Details |
| A | GLU269 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000255|PROSITE-ProRule:PRU10008, ECO:0000269|PubMed:3676276 |
| Chain | Residue | Details |
| A | CYS303 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 7 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25450233, ECO:0000269|PubMed:25634381, ECO:0007744|PDB:4WB9, ECO:0007744|PDB:4X4L |
| Chain | Residue | Details |
| A | ILE167 | |
| A | LYS193 | |
| A | GLY226 | |
| A | GLY246 | |
| A | GLU269 | |
| A | GLU349 | |
| A | GLU400 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P20000 |
| Chain | Residue | Details |
| A | ASN170 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylserine => ECO:0000269|PubMed:6723659, ECO:0007744|PubMed:22223895 |
| Chain | Residue | Details |
| A | SER2 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 9 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | LYS91 | |
| A | LYS128 | |
| A | LYS252 | |
| A | LYS353 | |
| A | LYS367 | |
| A | LYS410 | |
| A | LYS419 | |
| A | LYS435 | |
| A | LYS495 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | THR337 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SER413 |
