Crystal structure of human aldehyde dehydrogenase 1A3 in complex with a selective inhibitor

Structure

x-ray diffraction · 3 distinct chains · 41% helix, 22% strand (DSSP).

Ligands and binding sites

• NAD · Nicotinamide-adenine-dinucleotide · ligand · 4 copies · chains A, B, C, D
• N98 · methyl 5-(1,3-benzodioxol-5-yl)-2-phenyl-pyrazolo[1,5-a]pyrimidine-7-carboxylate · ligand · 4 copies · chains A, B, C, D

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

20 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.

Interfaces

6 interfaces between chains.

• B–D · 2799 Ų buried · 63 hydrogen bonds · protein-protein
• A–C · 2776 Ų buried · 60 hydrogen bonds · protein-protein
• A–D · 1090 Ų buried · 9 hydrogen bonds · protein-protein
• B–C · 1069 Ų buried · 13 hydrogen bonds · protein-protein
• A–B · 1030 Ų buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

• 6TGW · Crystal structure of human Aldehyde dehydrogenase 1A3 in complex with a selective… · the same entry in another collection · chain D against D, TM-score 1.00
• P47895 · AlphaFold monomer V2.0 prediction for aldehyde dehydrogenase family 1 member A3 (P47895) · a predicted model of the same protein · chain D against A, TM-score 1.00

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt P47895
• Elsewhere: RCSB PDB 6TGW · PDBe 6TGW · UniProt P47895