› 1ppd

X-ray diffraction
2Å resolution

RESTRAINED LEAST-SQUARES REFINEMENT OF THE SULFHYDRYL PROTEASE PAPAIN TO 2.0 ANGSTROMS

Released:
DOI: 10.2210/pdb1ppd/pdb
PDB entry 1ppd coloured by chain, front view.
PDB entry 1ppd coloured by chain, side view.
PDB entry 1ppd coloured by chain, top view.
Source organism: Carica papaya
Primary publication:
Restrained Least-Squares Refinement of the Sulfhydryl Protease Papain to 2.0 Angstroms
Priestle JP, Ford GC, Glor M, Mehler EL, Smit JDG, Thaller C, Jansonius JN
Acta Crystallogr., A, Found. Crystallogr. 40 17- (1984)

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: 23.45 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 BME 1 x BME
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 42.8Å b: 95.7Å c: 49.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.145 not available not available
Expression system: Not provided

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