› 3pa7

X-ray diffraction
2.61Å resolution

Crystal structure of FKBP from plasmodium vivax in complex with tetrapeptide ALPF

Released:
DOI: 10.2210/pdb3pa7/pdb
PDB entry 3pa7 coloured by chain, front view.
PDB entry 3pa7 coloured by chain, side view.
PDB entry 3pa7 coloured by chain, top view.
Source organism: Plasmodium vivax
Primary publication:
Structural insights into substrate binding by PvFKBP35, a peptidylprolyl cis-trans isomerase from the human malarial parasite Plasmodium vivax.
Alag R, Balakrishna AM, Rajan S, Qureshi IA, Shin J, Lescar J, Grüber G, Yoon HS
Eukaryot Cell 12 627-34 (2013)
PMID: 23435727

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:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-107694 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
peptidylprolyl isomerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 126 amino acids
Theoretical weight: 13.97 KDa
Source organism: Plasmodium vivax
Expression system: Escherichia coli
UniProt:
  • Canonical: A5K8X6 (Residues: 1-126; Coverage: 42%)
Gene name: PVX_101260
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase
Structure domains: Chitinase A; domain 3
4-mer Peptide ALPF Chain: D
Molecule details ›
Chain: D
Length: 4 amino acids
Theoretical weight: 447 Da
Source organism: Plasmodium vivax
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: C2
Unit cell:
a: 88.963Å b: 41.378Å c: 61.303Å
α: 90° β: 95.02° γ: 90°
R-values:
R R work R free
0.242 0.237 0.287
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

3 review citations

AIPL1: A specialized chaperone for the phototransduction effector.
Yadav et al. (2017)
2 more

1 mention without citation

Discovery of Novel µ-Opioid Receptor Inverse Agonist from a Combinatorial Library of Tetrapeptides through Structure-Based Virtual Screening.
Poli et al. (2019)