› 2haq

X-ray diffraction
1.97Å resolution

Crystal Structure of Cyclophilin A from Leishmania Donovani

Released:
DOI: 10.2210/pdb2haq/pdb
PDB entry 2haq coloured by chain, front view.
PDB entry 2haq coloured by chain, side view.
PDB entry 2haq coloured by chain, top view.
Source organism: Leishmania donovani
Primary publication:
Structure of cyclophilin from Leishmania donovani at 1.97 A resolution.
Venugopal V, Sen B, Datta AK, Banerjee R
Acta Crystallogr Sect F Struct Biol Cryst Commun 63 60-4 (2007)
PMID: 17277440

Function and Biology Details

Reaction catalysed: 
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193639 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase Chain: A
Molecule details ›
Chain: A
Length: 172 amino acids
Theoretical weight: 19.09 KDa
Source organism: Leishmania donovani
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9U9R3 (Residues: 22-187; Coverage: 100%)
Gene name: CYP
Sequence domains: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD
Structure domains: Cyclophilin-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P43212
Unit cell:
a: 48.59Å b: 48.59Å c: 141.19Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 0.178 0.197
Expression system: Escherichia coli

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Citations

1 citations in other articles

Interactions of antiparasitic alkaloids with Leishmania protein targets: a molecular docking analysis.
Ogungbe et al. (2013)

7 mentions without citation

The Potential of Secondary Metabolites from Plants as Drugs or Leads against Protozoan Neglected Diseases-Part III: In-Silico Molecular Docking Investigations.
Ogungbe et al. (2016)
6 more