› 2aim

X-ray diffraction
2.2Å resolution

CRUZAIN INHIBITED WITH BENZOYL-ARGININE-ALANINE-FLUOROMETHYLKETONE

Released:
DOI: 10.2210/pdb2aim/pdb
PDB entry 2aim coloured by chain, front view.
PDB entry 2aim coloured by chain, side view.
PDB entry 2aim coloured by chain, top view.
Source organism: Trypanosoma cruzi
Primary publication:
Structural determinants of specificity in the cysteine protease cruzain.
Gillmor SA, Craik CS, Fletterick RJ
Protein Sci 6 1603-11 (1997)
PMID: 9260273

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 ZRA 1 x ZRA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21
Unit cell:
a: 43.16Å b: 51.6Å c: 45.2Å
α: 90° β: 115.2° γ: 90°
R-values:
R R work R free
0.186 0.186 0.249
Expression system: Escherichia coli

Quick links

Citations

13 review citations

The lysosomal cysteine proteases.
McGrath ME. (1999)
12 more

9 mentions without citation

The Potential of Secondary Metabolites from Plants as Drugs or Leads against Protozoan Neglected Diseases-Part III: In-Silico Molecular Docking Investigations.
Ogungbe et al. (2016)
8 more