1cyn Summary

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CYCLOPHILIN B COMPLEXED WITH [D-(CHOLINYLESTER)SER8]-CYCLOSPORIN

The structure was published by Mikol, V., Kallen, J., and Walkinshaw, M.D., in 1994 in a paper entitled "X-Ray Structure of a Cyclophilin B/Cyclosporin Complex: Comparison with Cyclophilin a and Delineation of its Calcineurin-Binding Domain." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.85 Å and deposited in 1995.

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 B 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 B P23284 (39-216) (PPIB_HUMAN)search Homo sapienssearch 97% 178 100%
C CYCLOSPORIN A Not available
TOLYPOCLADIUM INFLATUMsearch Not available 11 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P23284 (39 - 216) PEPTIDYL-PROLYL CIS-TRANS ISOMERASE B Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P23284) Cyclophilin (peptidylprolyl isomerase)search Cyclophilinsearch PF00160: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLDsearch
C

Chain Molecule NORINE reference
CCYCLOSPORIN ANOR00033

Chain ID Cellular component (GO) Molecular function (GO) Biological process (GO)
A (P23284) endoplasmic reticulumsearch endoplasmic reticulum lumensearch extracellular vesicular exosomesearch melanosomesearch nucleussearch macromolecular complexsearch membranesearch focal adhesionsearch unfolded protein bindingsearch peptidyl-prolyl cis-trans isomerase activitysearch collagen bindingsearch poly(A) RNA bindingsearch protein bindingsearch isomerase activitysearch peptide bindingsearch protein complex bindingsearch protein stabilizationsearch bone developmentsearch extracellular matrix organizationsearch protein foldingsearch protein peptidyl-prolyl isomerizationsearch regulation of post-translational protein modificationsearch positive regulation of multicellular organism growthsearch chaperone-mediated protein foldingsearch

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