Five atomic resolution structures of endothiapepsin inhibitor complexes; implications for the aspartic proteinase mechanism

Structure

x-ray diffraction · 1 distinct chain · 10% helix, 45% strand (DSSP).

Ligands and binding sites

• SUI · (3-amino-2,5-dioxo-1-pyrrolidinyl)acetic acid · ligand · chains A
• 0GM · N-[(5S,9S,10S,13S)-9-hydroxy-5,10-bis(2-methylpropyl)-4,7,12,16-tetraoxo-3,6,11,17-tetraazabicyclo[17.3.1]tricosa-1(23),19,21-trien-13-yl]-3-(naphthalen-1-yl)-2-(naphthalen-1-ylmethyl)propanamide · ligand · chains A
• SO4 · Sulfate ion · ion · 2 copies · chains A

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: 2 covalent, 1 disulfide (covalent ligand, disulfide).

Compared structures

• 1GVV · Five Atomic Resolution Structures of Endothiapepsin Inhibitor Complexes; implications for… · the same entry in another collection · chain A against A, TM-score 1.00
• P11838 · AlphaFold monomer V2.0 prediction for endothiapepsin (P11838) · a predicted model of the same protein · chain A 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 1GVV · PDBe 1GVV · UniProt P11838