› 2vn1

X-ray diffraction
2.35Å resolution

Crystal structure of the FK506-binding domain of Plasmodium falciparum FKBP35 in complex with FK506

Released:
DOI: 10.2210/pdb2vn1/pdb
PDB entry 2vn1 coloured by chain, front view.
PDB entry 2vn1 coloured by chain, side view.
PDB entry 2vn1 coloured by chain, top view.
Source organism: Plasmodium falciparum 3D7
Primary publication:
Crystal structure of the FK506 binding domain of Plasmodium falciparum FKBP35 in complex with FK506.
Kotaka M, Ye H, Alag R, Hu G, Bozdech Z, Preiser PR, Yoon HS, Lescar J
Biochemistry 47 5951-61 (2008)
PMID: 18465874

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184673 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase FKBP35 Chains: A, B
Molecule details ›
Chains: A, B
Length: 129 amino acids
Theoretical weight: 14.53 KDa
Source organism: Plasmodium falciparum 3D7
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8I4V8 (Residues: 1-127; Coverage: 42%)
Gene names: FKBP35, PF3D7_1247400
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase
Structure domains: Chitinase A; domain 3

Ligands and Environments

1 bound ligand:
Ligand FK5 2 x FK5
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P43212
Unit cell:
a: 63.064Å b: 63.064Å c: 167.99Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.194 0.25
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

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

8 mentions without citation

Structural insights into Plasmodium PPIases.
Rajan et al. (2022)
7 more