Human aldehyde dehydrogenase 1A1 with duocarmycin analog

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 22% strand (DSSP).

Ligands and binding sites

• K9P · 1-[(1S)-1-methyl-5-oxidanyl-1,2-dihydrobenzo[e]indol-3-yl]hexan-1-one · ligand · chains A
• TXE · [[(2R,3S,4R,5R)-5-[(3R)-3-aminocarbonyl-3,4-dihydro-2H-pyridin-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanidyl-phosphoryl] [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl phosphate · ligand · chains A
• YB · Ytterbium (III) ion · metal · 3 copies · chains A

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

Pockets

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

Modifications

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

Compared structures

• 5AC2 · human aldehyde dehydrogenase 1A1 with duocarmycin analog · the same entry in another collection · chain A against A, TM-score 1.00
• P00352 · AlphaFold monomer V2.0 prediction for retinal dehydrogenase 1 (P00352) · a predicted model of the same protein · chain A 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 P00352
• Elsewhere: RCSB PDB 5AC2 · PDBe 5AC2 · UniProt P00352