High-resolution X-ray diffraction study of the complex between endothiapepsin and an oligopeptide inhibitor. the analysis of the inhibitor binding and description of the rigid body shift in the enzyme

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 46% strand (DSSP).

Ligands and binding sites

• 0EK · 6-ammonio-N-{[(2R,3R)-3-{[N-(tert-butoxycarbonyl)-L-phenylalanyl-3-(1H-imidazol-3-ium-4-yl)-L-alanyl]amino}-4-cyclohexyl-2-hydroxybutyl](2-methylpropyl)carbamoyl}-L-norleucyl-L-phenylalanine · ligand · chains E

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

Pockets

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

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

• 5ER2 · High-resolution X-ray diffraction study of the complex between endothiapepsin and an… · the same entry in another collection · chain E against E, TM-score 1.00
• P11838 · AlphaFold monomer V2.0 prediction for endothiapepsin (P11838) · a predicted model of the same protein · chain E against A, TM-score 0.99

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 P11838
• Elsewhere: RCSB PDB 5ER2 · PDBe 5ER2 · UniProt P11838