1meg

X-ray diffraction
2Å resolution

CRYSTAL STRUCTURE OF A CARICAIN D158E MUTANT IN COMPLEX WITH E-64

Released:

Function and Biology Details

Reaction catalysed:
Hydrolysis of proteins with broad specificity for peptide bonds, similar to those of papain and chymopapain.
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145152 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Caricain Chain: A
Molecule details ›
Chain: A
Length: 216 amino acids
Theoretical weight: 23.34 KDa
Source organism: Carica papaya
Expression system: Escherichia coli
UniProt:
  • Canonical: P10056 (Residues: 133-348; Coverage: 65%)
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: C2
Unit cell:
a: 53.45Å b: 65.33Å c: 64.37Å
α: 90° β: 111.6° γ: 90°
R-values:
R R work R free
0.193 0.193 not available
Expression system: Escherichia coli