1xyh Summary


Crystal Structure of Recombinant Human Cyclophilin J

The structure was published by Huang, L.L., Zhao, X.M., Huang, C.Q., Yu, L., and Xia, Z.X., in 2005 in a paper entitled "Structure of recombinant human cyclophilin J, a novel member of the cyclophilin family." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.6 Å and deposited in 2004.

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

The PDB entry contains the structure of cyclophilin-like protein PPIL3b. This molecule has the UniProt identifier Q9H2H8 (PPIL3_HUMAN)search. The sample contained 161 residues which is 100% of the natural sequence. Out of 161 residues 160 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
A cyclophilin-like protein PPIL3b Q9H2H8 (1-161) (PPIL3_HUMAN)search Homo sapienssearch 100% 161 99%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q9H2H8 (1 - 161) cyclophilin-like protein PPIL3b Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (Q9H2H8) Cyclophilin (peptidylprolyl isomerase)search Cyclophilinsearch PF00160: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLDsearch

Chain ID Biological process (GO) Molecular function (GO) Cellular component (GO)
A (Q9H2H8) protein foldingsearch protein peptidyl-prolyl isomerizationsearch mRNA processingsearch mRNA splicing, via spliceosomesearch RNA splicingsearch peptidyl-prolyl cis-trans isomerase activitysearch protein bindingsearch isomerase activitysearch catalytic step 2 spliceosomesearch spliceosomal complexsearch

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