› 1ewp

X-ray diffraction
1.75Å resolution

CRUZAIN BOUND TO MOR-LEU-HPQ

Released:
DOI: 10.2210/pdb1ewp/pdb
PDB entry 1ewp coloured by chain, front view.
PDB entry 1ewp coloured by chain, side view.
PDB entry 1ewp coloured by chain, top view.
Source organism: Trypanosoma cruzi
Primary publication:
Chapter 3: X-ray Structures of Complexes of Cruzain with Designed Covalent Inhibitors
Gillmor SA
Enzyme-ligand Interactions, Inhibition and Specificity 50-80 (1998)

Function and Biology Details

Reaction catalysed: 
Broad endopeptidase specificity similar to that of cathepsin L.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150579 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cruzipain Chain: A
Molecule details ›
Chain: A
Length: 215 amino acids
Theoretical weight: 22.72 KDa
Source organism: Trypanosoma cruzi
Expression system: Escherichia coli
UniProt:
  • Canonical: P25779 (Residues: 123-337; Coverage: 48%)
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases

Ligands and Environments

1 bound ligand:
Ligand 0I5 1 x 0I5
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 43.511Å b: 51.654Å c: 45.259Å
α: 90° β: 114.76° γ: 90°
R-values:
R R work R free
0.19 0.183 0.206
Expression system: Escherichia coli

Quick links

Citations

5 mentions without citation

The cathepsin L of Toxoplasma gondii (TgCPL) and its endogenous macromolecular inhibitor, toxostatin.
Huang et al. (2009)
4 more