1qng Summary

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Plasmodium falciparum Cyclophilin complexed with Cyclosporin A

The structure was published by Peterson, M.R., Hall, D.R., Berriman, M., Leonard, G.A., Fairlamb, A.H., and Hunter, W.N., in 2000 in a paper entitled "The Three-Dimensional Structure of a Plasmodium Falciparum Cyclophilin in Complex with the Potent Anti-Malarial Cyclosporin A" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.1 Å and deposited in 1999.

The experimental data on which the structure is based was also deposited.

This PDB entry contains a complex of 2 biomacromolecules, namely PEPTIDYL-PROLYL CIS-TRANS ISOMERASE and CYCLOSPORIN A.

The molecule most likely forms heterodimers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A PEPTIDYL-PROLYL CIS-TRANS ISOMERASE Q25756 (2-171) (Q25756_PLAFA)search Plasmodium falciparumsearch 99% 170 100%
D CYCLOSPORIN A Not available
Tolypocladium inflatumsearch Not available 11 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q25756 (2 - 171) PEPTIDYL-PROLYL CIS-TRANS ISOMERASE Plasmodium falciparum

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (Q25756) Cyclophilin (peptidylprolyl isomerase)search Cyclophilinsearch PF00160: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLDsearch
D

Chain Molecule NORINE reference
DCYCLOSPORIN ANOR00033

Chain ID Biological process (GO) Molecular function (GO)
A (Q25756) protein peptidyl-prolyl isomerizationsearch protein foldingsearch isomerase activitysearch peptidyl-prolyl cis-trans isomerase activitysearch

Chain InterPro annotation
A Cyclophilin-type peptidyl-prolyl cis-trans isomerase domainsearch Cyclophilin-type peptidyl-prolyl cis-trans isomerase, conserved sitesearch Cyclophilin-type peptidyl-prolyl cis-trans isomerasesearch Cyclophilin-like domainsearch
D