3qyu Summary


Crystal structure of human cyclophilin D at 1.54 A resolution at room temperature

The structure was published by le Maire, A., Gelin, M., Pochet, S., et al., Guichou, J.F., Ferrer, J.L., and Labesse, G., in 2011 in a paper entitled "In-plate protein crystallization, in situ ligand soaking and X-ray diffraction." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.54 Å and deposited in 2011.

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

The PDB entry contains the structure of Peptidyl-prolyl cis-trans isomerase F. This molecule has the UniProt identifier P30405 (PPIF_HUMAN)search. The sample contained 164 residues which is < 90% of the natural sequence. Out of 164 residues 163 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 Peptidyl-prolyl cis-trans isomerase F P30405 (44-207) (PPIF_HUMAN)search Homo sapienssearch < 90% 164 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P30405 (44 - 207) Peptidyl-prolyl cis-trans isomerase F Homo sapiens

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

Chain ID Molecular function (GO) Biological process (GO)
A (P30405) peptidyl-prolyl cis-trans isomerase activitysearch protein peptidyl-prolyl isomerizationsearch protein foldingsearch

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