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

Structure

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

Ligands and binding sites

• TCK · N-[(1S)-5-amino-1-(chloroacetyl)pentyl]-4-methylbenzenesulfonamide · ligand · chains B
• NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A, B
• FUC · alpha-L-fucopyranose · sugar · 2 copies · chains B
• BMA · beta-D-mannopyranose · sugar
• XYS · alpha-D-xylopyranose · sugar
• MAN · alpha-D-mannopyranose · sugar
• IPA · Isopropyl alcohol · additive · 2 copies · chains A
• CIT · Citric acid · additive · 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.

Interfaces

1 interface between chains.

• A–B · 582 Ų buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide, 2 glycan, 1 covalent (disulfide, N-glycosylation, covalent ligand).

Compared structures

• 6YCG · Structure the bromelain protease from Ananas comosus in complex with the TLCK 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 6YCG · PDBe 6YCG · UniProt O23799