PDBe 2pns

X-ray diffraction
1.9Å resolution

1.9 Angstrom resolution crystal structure of a plant cysteine protease Ervatamin-C refinement with cDNA derived amino acid sequence

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: P83654 (Residues: 1-208; 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: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 43.729Å b: 82.691Å c: 133.048Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.173 0.173 0.193