PDBe 1iwd

X-ray diffraction
1.63Å resolution

Proposed Amino Acid Sequence and the 1.63 Angstrom X-ray Crystal Structure of a Plant Cysteine Protease Ervatamin B: Insight into the Structural Basis of its Stability and Substrate Specificity.

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ervatamin-B Chain: A
Molecule details ›
Chain: A
Length: 215 amino acids
Theoretical weight: 23.2 KDa
Source organism: Tabernaemontana divaricata
UniProt:
  • Canonical: P60994 (Residues: 1-215; Coverage: 100%)
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 48.2Å b: 58.76Å c: 69.35Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.163 0.161 0.184