› 2pre

X-ray diffraction
2.7Å resolution

Crystal structure of plant cysteine protease Ervatamin-C complexed with irreversible inhibitor E-64 at 2.7 A resolution

Released:
DOI: 10.2210/pdb2pre/pdb
PDB entry 2pre coloured by chain, front view.
PDB entry 2pre coloured by chain, side view.
PDB entry 2pre coloured by chain, top view.
Source organism: Tabernaemontana divaricata
Primary publication:
Structural insights into the substrate specificity and activity of ervatamins, the papain-like cysteine proteases from a tropical plant, Ervatamia coronaria.
Ghosh R, Chakraborty S, Chakrabarti C, Dattagupta JK, Biswas S
FEBS J 275 421-34 (2008)
PMID: 18167146

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-108611 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ervatamin-C Chains: A, B
Molecule details ›
Chains: A, B
Length: 208 amino acids
Theoretical weight: 22.99 KDa
Source organism: Tabernaemontana divaricata
UniProt:
  • Canonical: A8DS38 (Residues: 134-341; Coverage: 60%)
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases

Ligands and Environments

2 bound ligands:
Ligand SO4 6 x SO4
Ligand E64 2 x E64
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR
Spacegroup: P212121
Unit cell:
a: 43.37Å b: 81.46Å c: 131.95Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.197 0.234

Quick links

Citations

6 citation in other articles

Subclassification and biochemical analysis of plant papain-like cysteine proteases displays subfamily-specific characteristics.
Richau et al. (2012)
5 more

4 mentions without citation

A non-canonical DNA structure enables homologous recombination in various genetic systems.
Masuda et al. (2009)
3 more