1w8m Summary

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ENZYMATIC AND STRUCTURAL CHARACTERISATION OF NON PEPTIDE LIGAND CYCLOPHILIN COMPLEXES

The structure was published by Kontopidis, G., Taylor, P., and Walkinshaw, M., in 2004 in a paper entitled "Enzymatic and Structural Characterization of Non-Peptide Ligand-Cyclophilin Complexes" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.65 Å and deposited in 2004.

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

The PDB entry contains the structure of PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A.

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 A P62937 (2-165) (PPIA_HUMAN)search Homo sapienssearch 99% 165 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P62937 (2 - 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 Cyclophilin-likesearch PF00160: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLDsearch

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

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