PDBe 3p5x

X-ray diffraction
2.2Å resolution

Actinidin from Actinidia arguta planch (Sarusashi)

Released:

Function and Biology Details

Reaction catalysed:
Specificity close to that of papain. 
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Actinidin Act1b Chain: A
Molecule details ›
Chain: A
Length: 220 amino acids
Theoretical weight: 23.99 KDa
Source organism: Actinidia arguta
UniProt:
  • Canonical: A5HII2 (Residues: 127-346; Coverage: 62%)
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E DW
Spacegroup: P212121
Unit cell:
a: 48.519Å b: 56.039Å c: 70.916Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.168 0.222