› 2act

X-ray diffraction
1.7Å resolution

CRYSTALLOGRAPHIC REFINEMENT OF THE STRUCTURE OF ACTINIDIN AT 1.7 ANGSTROMS RESOLUTION BY FAST FOURIER LEAST-SQUARES METHODS

Released:
DOI: 10.2210/pdb2act/pdb
PDB entry 2act coloured by chain, front view.
PDB entry 2act coloured by chain, side view.
PDB entry 2act coloured by chain, top view.
Source organism: Actinidia chinensis
Primary publication:
Crystallographic Refinement of the Structure of Actinidin at 1.7 Angstroms Resolution by Fast Fourier Least-Squares Methods
Baker EN, Dodson EJ
Acta Crystallogr., A, Found. Crystallogr. 36 559- (1980)

Function and Biology Details

Reaction catalysed: 
Similar to that of papain.
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-133550 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Actinidain Chain: A
Molecule details ›
Chain: A
Length: 220 amino acids
Theoretical weight: 23.72 KDa
Source organism: Actinidia chinensis
Expression system: Not provided
UniProt:
  • Canonical: P00785 (Residues: 127-346; Coverage: 62%)
Gene names: ACT1A, CEY00_Acc12058
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases

Ligands and Environments

1 bound ligand:
Ligand NH4 1 x NH4
1 modified residue:
Ligand CSD 1 x CSD

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 78.2Å b: 81.8Å c: 33.03Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.171 not available
Expression system: Not provided

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Citations

23 mentions without citation

Molecular docking: a powerful approach for structure-based drug discovery.
Meng et al. (2011)
22 more