4WP7
Structure of human ALDH1A1 with inhibitor CM026
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 (NAD+) 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 | 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 | 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 |
| A | 0140087 | molecular_function | acetaldehyde dehydrogenase (NAD+) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | binding site for residue YB A 601 |
| Chain | Residue |
| A | HOH714 |
| A | HOH781 |
| A | HOH781 |
| A | HOH792 |
| A | HOH936 |
| A | HOH939 |
| A | HOH940 |
| A | HOH941 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | binding site for residue 3SR A 602 |
| Chain | Residue |
| A | GLY125 |
| A | THR129 |
| A | PHE171 |
| A | TRP178 |
| A | HIS293 |
| A | GLY294 |
| A | TYR297 |
| A | CYS302 |
| A | ILE304 |
| A | GLY458 |
| A | VAL460 |
| A | ALA462 |
| A | HOH896 |
| A | SER121 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 603 |
| Chain | Residue |
| A | ARG143 |
| A | THR155 |
| A | HIS157 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | binding site for residue YB A 604 |
| Chain | Residue |
| A | HOH778 |
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 | 165 |
| Details | Region: {"description":"Mediates interaction with PRMT3","evidences":[{"source":"PubMed","id":"33495566","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10007","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10008","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"3676276","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10007","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10008","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"3676276","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25450233","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25634381","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4WB9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4X4L","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P20000","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 9 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
