Crystal structure of wild-type human pro-cathepsin H

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 19% strand (DSSP).

Ligands and binding sites

• NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A
• MAN · alpha-D-mannopyranose · sugar · 2 copies · chains A
• BMA · beta-D-mannopyranose · sugar · chains A
• SO4 · Sulfate ion · ion · 4 copies · chains A
• GOL · Glycerol · additive · 3 copies · chains A

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Modifications

Observed in the structure: 4 disulfide, 2 glycan, 1 modified (disulfide, N-glycosylation, oxidation).

Compared structures

• 6CZK · Crystal structure of wild-type human pro-cathepsin H · the same entry in another collection · chain A against A, TM-score 1.00
• P09668 · AlphaFold monomer V2.0 prediction for pro-cathepsin H (P09668) · 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 P09668
• Elsewhere: RCSB PDB 6CZK · PDBe 6CZK · UniProt P09668