1cwf Summary

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HUMAN CYCLOPHILIN A COMPLEXED WITH 2-VAL CYCLOSPORIN

The structure was published by Kallen, J., Mikol, V., Taylor, P., and Walkinshaw, M.D., in 1998 in a paper entitled "X-Ray Structures and Analysis of 11 Cyclosporin Derivatives Complexed with Cyclophilin A." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.86 Å and deposited in 1998.

The experimental data on which the structure is based was not deposited.

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

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 A P62937 (1-165) (PPIA_HUMAN)search Homo sapienssearch 99% 165 100%
C CYCLOSPORIN D Not available
TOLYPOCLADIUM INFLATUMsearch Not available 11 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P62937 (1 - 165) PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P62937) Cyclophilin (peptidylprolyl isomerase)search Cyclophilinsearch PF00160: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLDsearch
C

Chain Molecule NORINE reference
CCYCLOSPORIN DNOR00036

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A (P62937) peptidyl-prolyl cis-trans isomerase activitysearch protein bindingsearch isomerase activitysearch poly(A) RNA bindingsearch virion bindingsearch unfolded protein bindingsearch peptide bindingsearch protein foldingsearch RNA-dependent DNA replicationsearch platelet activationsearch viral processsearch leukocyte migrationsearch virion assemblysearch protein peptidyl-prolyl isomerizationsearch regulation of viral genome replicationsearch entry into host cellsearch blood coagulationsearch positive regulation of protein secretionsearch establishment of integrated proviral latencysearch lipid particle organizationsearch viral release from host cellsearch platelet degranulationsearch positive regulation of viral genome replicationsearch uncoating of virussearch viral life cyclesearch extracellular regionsearch cytosolsearch extracellular vesicular exosomesearch cytoplasmsearch focal adhesionsearch membranesearch nucleussearch extracellular spacesearch

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
C