PDBe 4kp9

X-ray diffraction
2.1Å resolution

Crystal structure of Papain modify by achiral Ru(II)complex

Released:
Source organism: Carica papaya
Entry authors: Cherrier MV, Madern N, Amara P, Salmain M, Fontecilla-Camps JC

Function and Biology Details

Reaction catalysed:
Hydrolysis of proteins with broad specificity for peptide bonds, but preference for an amino acid bearing a large hydrophobic side chain at the P2 position. Does not accept Val in P1'. 
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Papain Chain: A
Molecule details ›
Chain: A
Length: 212 amino acids
Theoretical weight: 23.48 KDa
Source organism: Carica papaya
UniProt:
  • Canonical: P00784 (Residues: 134-345; Coverage: 65%)
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases
Papain Chain: B
Molecule details ›
Chain: B
Length: 212 amino acids
Theoretical weight: 23.45 KDa
Source organism: Carica papaya
UniProt:
  • Canonical: P00784 (Residues: 134-345; Coverage: 65%)
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases

Ligands and Environments

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P212121
Unit cell:
a: 61.03Å b: 74.85Å c: 86.25Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.194 0.252