2alf Summary


crystal structure of human CypA mutant K131A

The structure was published by Hu, H., Huang, C.-Q., Liu, H.-L., et al., Chen, M.-E., Yu, L., and Bi, R.-C., in in a paper entitled "Nuclease activity of Cyclophilin A and its structural basis" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.9 Å and deposited in 2005.

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 164 residues which is 99% of the natural sequence. Out of 164 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 A P62937 (2-165) (PPIA_HUMAN)search Homo sapienssearch 99% 164 100%

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 Cyclophilinsearch PF00160: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLDsearch

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

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