2x25 Summary



The structure was published by Lammers, M., Neumann, H., Chin, J.W., and James, L.C., in 2010 in a paper entitled "Acetylation Regulates Cyclophilin a Catalysis, Immunosuppression and HIV Isomerization." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.2 Å and deposited in 2010.

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

The PDB entry contains the structure of PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A. This molecule has the UniProt identifier P62937 (PPIA_HUMAN)search. The sample contained 169 residues which is 99% of the natural sequence. Out of 169 residues 168 were observed and are deposited in the PDB.

The molecule is most likely monomeric.

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
B PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A P62937 (2-165) (PPIA_HUMAN)search Homo sapienssearch 99% 169 99%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB

Chain Sequence family (Pfam)
B (P62937) PF00160: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLDsearch

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

Chain InterPro annotation
B 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