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.; Tempel, W.; Davis, T.; Newman, E.M.; Finerty Jr., P.J.; Mackenzie, F.; Weigelt, J.; Sundstrom, M.; Arrowsmith, C.H.; Edwards, A.M.; Bochkarev, A.; Dhe-Paganon, S.; Structural Genomics Consortium (SGC)
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). 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):
This entry contains 1 unique UniProt protein: