X-ray diffraction
1.7Å resolution

Crystal Structure of the first nucleotide binding domain of chaperone ClpB1, putative, (Pv089580) from Plasmodium Vivax

Source organism: Plasmodium falciparum
Entry authors: Wernimont AK, Lew J, Kozieradzki I, Lin YH, Hassanali A, Zhao Y, Arrowsmith CH, Edwards AM, Weigelt J, Sundstrom M, Bochkarev A, Hui R, Artz JD, Structural Genomics Consortium (SGC)

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Clp R domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 187 amino acids
Theoretical weight: 20.44 KDa
Source organism: Plasmodium falciparum
Expression system: Escherichia coli
  • Canonical: Q8IB03 (Residues: 310-496; Coverage: 18%)
Gene name: PF3D7_0816600
Sequence domains: ATPase family associated with various cellular activities (AAA)
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 31.728Å b: 52.213Å c: 91.92Å
α: 90° β: 90° γ: 90°
R R work R free
0.203 0.201 0.239
Expression system: Escherichia coli