PDBe 3bcn

X-ray diffraction
2.85Å resolution

Crystal structure of a papain-like cysteine protease Ervatamin-A complexed with irreversible inhibitor E-64

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ervatamin-A Chains: A, B
Molecule details ›
Chains: A, B
Length: 209 amino acids
Theoretical weight: 22.85 KDa
Source organism: Tabernaemontana divaricata
UniProt:
  • Canonical: A5YVK8 (Residues: 1-184; Coverage: 100%)
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: P21
Unit cell:
a: 31.168Å b: 105.587Å c: 73.927Å
α: 90° β: 101.96° γ: 90°
R-values:
R R work R free
0.24 0.24 0.27