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:
Biological process:
Cellular component:
- not assigned
Sequence domains:
Structure domain:
Structure analysis Details
Assemblies composition:
Assembly name:
Gastricsin (preferred)
PDBe Complex ID:
PDB-CPX-148859 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Gastricsin
Molecule details ›
Chain: P
Length: 43 amino acids
Theoretical weight: 5.14 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
Sequence domains: A1 Propeptide
Structure domains: Helix Hairpins
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%)
Sequence domains: A1 Propeptide
Structure domains: Helix Hairpins
Gastricsin
Molecule details ›
Chain: B
Length: 329 amino acids
Theoretical weight: 35.46 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases
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%)
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Spacegroup:
P42212
Expression system: Not provided
