PDBe 1pad

X-ray diffraction
2.8Å resolution

Binding of chloromethyl ketone substrate analogues to crystalline papain

Released:
Primary publication:
Binding of chloromethyl ketone substrate analogues to crystalline papain.
Biochemistry 15 3731-8 (1976)
PMID: 952885

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: 23.45 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
ACETYL-ALA-ALA-PHE-ALA-CHLOROMETHYLKETONE INHIBITOR Chain: I
Molecule details ›
Chain: I
Length: 6 amino acids
Theoretical weight: 437 Da
Source organism: Synthetic construct
Expression system: Not provided

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 45Å b: 104.3Å c: 50.8Å
α: 90° β: 90° γ: 90°
Expression system: Not provided