2zr5 Summary


Crystal structure of a mutant PIN1 peptidyl-prolyl cis-trans isomerase

A publication describing this structure is not available. The depositing authors are Jobichen, C.search; Yih-Cherng, L.search; Sivaraman, J.search

This crystal structure was determined using X-ray diffraction at a resolution of 2.6 Å and deposited in 2008.

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 1. This molecule has the UniProt identifier Q13526 (PIN1_HUMAN)search. The sample contained 163 residues which is 100% of the natural sequence. Out of 163 residues 152 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 1 Q13526 (1-163) (PIN1_HUMAN)search Homo sapienssearch 96% 163 93%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q13526 (1 - 163) Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 Homo sapiens

Chain Structural classification (CATH) Sequence family (Pfam)
A (Q13526) Ubiquitin Ligase Nedd4; Chain: W;search, Chitinase A; domain 3search PF00397: WW domainsearch, PF00639: PPIC-type PPIASE domainsearch

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A (Q13526) protein bindingsearch isomerase activitysearch peptidyl-prolyl cis-trans isomerase activitysearch GTPase activating protein bindingsearch phosphoserine bindingsearch mitogen-activated protein kinase kinase bindingsearch phosphothreonine bindingsearch regulation of cytokinesissearch protein peptidyl-prolyl isomerizationsearch metabolic processsearch negative regulation of cell motilitysearch positive regulation of GTPase activitysearch negative regulation of transforming growth factor beta receptor signaling pathwaysearch positive regulation of protein phosphorylationsearch regulation of mitotic nuclear divisionsearch negative regulation of ERK1 and ERK2 cascadesearch negative regulation of type I interferon productionsearch innate immune responsesearch cell cyclesearch cytokine-mediated signaling pathwaysearch regulation of pathway-restricted SMAD protein phosphorylationsearch positive regulation of ubiquitin-protein transferase activitysearch cytoplasmsearch nucleussearch nucleoplasmsearch midbodysearch nuclear specksearch

Chain InterPro annotation
A Peptidyl-prolyl cis-trans isomerase, PpiC-typesearch WW domainsearch Peptidyl-prolyl cis-trans isomerase, PpiC-type, conserved sitesearch