› 9pap

X-ray diffraction
1.65Å resolution

STRUCTURE OF PAPAIN REFINED AT 1.65 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb9pap/pdb
PDB entry 9pap coloured by chain, front view.
PDB entry 9pap coloured by chain, side view.
PDB entry 9pap coloured by chain, top view.
Source organism: Carica papaya
Primary publication:
Structure of papain refined at 1.65 A resolution.
Kamphuis IG, Kalk KH, Swarte MB, Drenth J
J Mol Biol 179 233-56 (1984)
PMID: 6502713

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
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133539 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Papain Chain: A
Molecule details ›
Chain: A
Length: 212 amino acids
Theoretical weight: 23.5 KDa
Source organism: Carica papaya
Expression system: Not provided
UniProt:
  • Canonical: P00784 (Residues: 134-345; Coverage: 65%)
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases

Ligands and Environments

1 bound ligand:
Ligand MOH 29 x MOH
1 modified residue:
Ligand OCS 1 x OCS

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 45.2Å b: 104.64Å c: 50.88Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.161 not available not available
Expression system: Not provided

Quick links

Citations

14 review citations

The lysosomal cysteine proteases.
McGrath ME. (1999)
13 more

41 mentions without citation

Cysteine cathepsins: from structure, function and regulation to new frontiers.
Turk et al. (2012)
40 more