PDBe 3ioq

X-ray diffraction
1.87Å resolution

Crystal structure of the Carica candamarcensis cysteine protease CMS1MS2 in complex with E-64.

Released:
Entry authors: Gomes MTR, Teixeira RD, Salas CE, Nagem RAP

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cysteine proteinase Chain: A
Molecule details ›
Chain: A
Length: 213 amino acids
Theoretical weight: 23.03 KDa
Source organism: Vasconcellea cundinamarcensis
UniProt:
  • Canonical: Q84XA1 (Residues: 2-172, 173-181; Coverage: 99%)
Structure domains: Cysteine proteinases

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LNLS BEAMLINE W01B-MX2
Spacegroup: P41212
Unit cell:
a: 73.639Å b: 73.639Å c: 118.786Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.164 0.162 0.193