Structure the bromelain protease from ananas comosus in complex with the E64 inhibitor

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 22% strand (DSSP).

Ligands and binding sites

• E64 · N-[N-[1-hydroxycarboxyethyl-carbonyl]leucylamino-butyl]-guanidine · ligand · 2 copies · chains A, B
• NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A, B
• BMA · beta-D-mannopyranose · sugar
• XYS · alpha-D-xylopyranose · sugar
• MAN · alpha-D-mannopyranose · sugar
• FUC · alpha-L-fucopyranose · sugar
• CIT · Citric acid · additive · chains A
• IPA · Isopropyl alcohol · additive · chains B

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

Pockets

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

Interfaces

1 interface between chains.

• A–B · 590 Ų buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide, 2 covalent, 2 glycan (disulfide, covalent ligand, N-glycosylation).

Compared structures

• 6YCF · Structure the bromelain protease from Ananas comosus in complex with the E64 inhibitor · the same entry in another collection · 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 O23799
• Elsewhere: RCSB PDB 6YCF · PDBe 6YCF · UniProt O23799