› 2fbn

X-ray diffraction
1.63Å resolution

Plasmodium falciparum putative FK506-binding protein PFL2275c, C-terminal TPR-containing domain

Released:
DOI: 10.2210/pdb2fbn/pdb
PDB entry 2fbn coloured by chain, front view.
PDB entry 2fbn coloured by chain, side view.
PDB entry 2fbn coloured by chain, top view.
Source organism: Plasmodium falciparum
Primary publication:
Crystallographic structure of the tetratricopeptide repeat domain of Plasmodium falciparum FKBP35 and its molecular interaction with Hsp90 C-terminal pentapeptide.
Alag R, Bharatham N, Dong A, Hills T, Harikishore A, Widjaja AA, Shochat SG, Hui R, Yoon HS
Protein Sci 18 2115-24 (2009)
PMID: 19691130

Function and Biology Details

Reaction catalysed: 
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184674 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase FKBP35 Chains: A, B
Molecule details ›
Chains: A, B
Length: 198 amino acids
Theoretical weight: 23.04 KDa
Source organism: Plasmodium falciparum
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q8I4V8 (Residues: 128-304; Coverage: 58%)
Gene names: FKBP35, PF3D7_1247400
Structure domains: Tetratricopeptide repeat domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E, RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 56.239Å b: 62.936Å c: 103.334Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.2 0.235
Expression system: Escherichia coli BL21

Quick links

Citations

5 review citations

Co-chaperones of Hsp90 in Plasmodium falciparum and their concerted roles in cellular regulation.
Chua et al. (2014)
4 more

5 mentions without citation

Robust structural analysis of native biological macromolecules from multi-crystal anomalous diffraction data.
Liu et al. (2013)
4 more