3ui4 Summary


0.8 A resolution crystal structure of human Parvulin 14

The structure was published by Mueller, J.W., Link, N.M., Matena, A., et al., Ruppel, A., Bayer, P., and Blankenfeldt, W., in 2011 in a paper entitled "Crystallographic proof for an extended hydrogen-bonding network in small prolyl isomerases." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 0.8 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 NIMA-interacting 4. This molecule has the UniProt identifier Q9Y237 (PIN4_HUMAN)search. The sample contained 101 residues which is < 90% of the natural sequence. Out of 101 residues 100 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 NIMA-interacting 4 Q9Y237 (36-131) (PIN4_HUMAN)search Homo sapienssearch < 90% 101 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q9Y237 (36 - 131) Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4 Homo sapiens

Chain Sequence family (Pfam)
A PPIC-type PPIASE domainsearch

Chain ID Molecular function (GO)
A (Q9Y237) isomerase activitysearch

Chain InterPro annotation
A Peptidyl-prolyl cis-trans isomerase, PpiC-typesearch