PDBe 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:

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (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:

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