PDBe 1htr

X-ray diffraction
1.62Å resolution

CRYSTAL AND MOLECULAR STRUCTURES OF HUMAN PROGASTRICSIN AT 1.62 ANGSTROMS RESOLUTION

Released:
Source organism: Homo sapiens

Function and Biology Details

Reaction catalysed:
More restricted specificity than pepsin A, but shows preferential cleavage at Tyr-|- bonds. High activity on hemoglobin.
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
hetero tetramer
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Gastricsin Chain: P
Molecule details ›
Chain: P
Length: 43 amino acids
Theoretical weight: 5.14 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P20142 (Residues: 17-59; Coverage: 12%)
Gene name: PGC
Sequence domains: A1 Propeptide
Gastricsin Chain: B
Molecule details ›
Chain: B
Length: 329 amino acids
Theoretical weight: 35.46 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P20142 (Residues: 60-388; Coverage: 88%)
Gene name: PGC
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P42212
Unit cell:
a: 105.31Å b: 105.31Å c: 70.42Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 not available not available
Expression system: Not provided