PDBe 3e1z

X-ray diffraction
1.86Å resolution

Crystal structure of the parasite protesase inhibitor chagasin in complex with papain

Released:

Function and Biology Details

Reaction catalysed:
Hydrolysis of proteins with broad specificity for peptide bonds, but preference for an amino acid bearing a large hydrophobic side chain at the P2 position. Does not accept Val in P1'. 
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Papain Chain: B
Molecule details ›
Chain: B
Length: 212 amino acids
Theoretical weight: 23.45 KDa
Source organism: Carica papaya
UniProt:
  • Canonical: P00784 (Residues: 134-345; Coverage: 65%)
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases
Chagasin Chain: A
Molecule details ›
Chain: A
Length: 110 amino acids
Theoretical weight: 12.05 KDa
Source organism: Trypanosoma cruzi
Expression system: Escherichia coli
UniProt:
  • Canonical: Q966X9 (Residues: 1-110; Coverage: 100%)
Gene name: cha
Sequence domains: Chagasin family peptidase inhibitor I42

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X13
Spacegroup: I422
Unit cell:
a: 99.13Å b: 99.13Å c: 159.49Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.166 0.164 0.208
Expression system: Escherichia coli