PDBe 1cqd

X-ray diffraction
2.1Å resolution

THE 2.1 ANGSTROM STRUCTURE OF A CYSTEINE PROTEASE WITH PROLINE SPECIFICITY FROM GINGER RHIZOME, ZINGIBER OFFICINALE

Released:

Function and Biology Details

Reaction catalysed:
Preferential cleavage of peptides with a proline residue at the P2 position. 
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Zingipain-2 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 221 amino acids
Theoretical weight: 23.94 KDa
Source organism: Zingiber officinale
UniProt:
  • Canonical: P82474 (Residues: 1-221; Coverage: 100%)
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P21
Unit cell:
a: 93.98Å b: 45.45Å c: 110.04Å
α: 90° β: 105.03° γ: 90°
R-values:
R R work R free
0.213 0.213 0.249