2gw2 Summary

pdbe.org/2gw2
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Crystal structure of the peptidyl-prolyl isomerase domain of human cyclophilin G

A publication describing this structure is not available. The depositing authors are Bernstein, G.search; Tempel, W.search; Davis, T.search; Newman, E.M.search; Finerty Jr., P.J.search; Mackenzie, F.search; Weigelt, J.search; Sundstrom, M.search; Arrowsmith, C.H.search; Edwards, A.M.search; Bochkarev, A.search; Dhe-Paganon, S.search; Structural Genomics Consortium (SGC)search

This crystal structure was determined using X-ray diffraction at a resolution of 1.8 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 G. This molecule has the UniProt identifier Q13427 (PPIG_HUMAN)search. The sample contained 198 residues which is < 90% of the natural sequence. Out of 198 residues 172 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 G Q13427 (1-179) (PPIG_HUMAN)search Homo sapienssearch < 90% 198 87%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q13427 (1 - 179) Peptidyl-prolyl cis-trans isomerase G Homo sapiens

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

Chain ID Biological process (GO) Molecular function (GO)
A (Q13427) protein peptidyl-prolyl isomerizationsearch protein foldingsearch peptidyl-prolyl cis-trans isomerase activitysearch

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