PDBe 8pch

X-ray diffraction
2.1Å resolution

CRYSTAL STRUCTURE OF PORCINE CATHEPSIN H DETERMINED AT 2.1 ANGSTROM RESOLUTION: LOCATION OF THE MINI-CHAIN C-TERMINAL CARBOXYL GROUP DEFINES CATHEPSIN H AMINOPEPTIDASE FUNCTION

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Cathepsin H Chain: A
Molecule details ›
Chain: A
Length: 220 amino acids
Theoretical weight: 24.33 KDa
Source organism: Sus scrofa
UniProt:
  • Canonical: O46427 (Residues: 116-335; Coverage: 70%)
Gene name: CTSH
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases
Cathepsin H mini chain Chain: P
Molecule details ›
Chain: P
Length: 8 amino acids
Theoretical weight: 849 Da
Source organism: Sus scrofa
UniProt:
  • Canonical: O46427 (Residues: 98-105; Coverage: 3%)
Gene name: CTSH

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P212121
Unit cell:
a: 38.442Å b: 68.73Å c: 86.757Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
not available not available 0.245