2cmt Summary

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THE STRUCTURE OF REDUCED CYCLOPHILIN A FROM S. MANSONI

The structure was published by Gourlay, L.J., Angelucci, F., Baiocco, P., et al., Brunori, M., Bellelli, A., and Miele, A.E., in 2007 in a paper entitled "The Three-Dimensional Structure of Two Redox States of Cyclophilin a from Schistosoma Mansoni. Evidence for Redox Regulation of Peptidyl-Prolyl Cis-Trans Isomerase Activity." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.5 Å and deposited in 2006.

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

The PDB entry contains the structure of PEPTIDYL-PROLYL CIS-TRANS ISOMERASE E. This molecule has the UniProt identifier Q26548 (PPIE_SCHMA)search. The sample contained 172 residues which is < 90% of the natural sequence. Out of 172 residues 164 were observed and are deposited in the PDB.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

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
A PEPTIDYL-PROLYL CIS-TRANS ISOMERASE E Q26548 (102-273) (PPIE_SCHMA)search Schistosoma mansonisearch < 90% 172 95%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q26548 (102 - 273) PEPTIDYL-PROLYL CIS-TRANS ISOMERASE E Schistosoma mansoni

Chain Sequence family (Pfam)
A Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLDsearch

Chain ID Molecular function (GO) Biological process (GO)
A (Q26548) peptidyl-prolyl cis-trans isomerase activitysearch protein foldingsearch protein peptidyl-prolyl isomerizationsearch

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