6czk

X-ray diffraction
2Å resolution

Crystal structure of wild-type human pro-cathepsin H

Released:
Source organism: Homo sapiens
Primary publication:
Crystal structures of human procathepsin H.
PLoS One 13 e0200374 (2018)
PMID: 30044821

Function and Biology Details

Reaction catalysed:
Hydrolysis of proteins, acting as an aminopeptidase (notably, cleaving Arg-|- bonds) as well as an endopeptidase.
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140729 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Pro-cathepsin H Chain: A
Molecule details ›
Chain: A
Length: 335 amino acids
Theoretical weight: 37.45 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P09668 (Residues: 1-335; Coverage: 100%)
Gene names: CPSB, CTSH
Sequence domains:
Structure domains: Cysteine proteinases

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer : NEW Components: NAG, BMA, MAN
2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P3121
Unit cell:
a: 97.416Å b: 97.416Å c: 107.53Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.172 0.17 0.2
Expression system: Spodoptera frugiperda