2zr6 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 3.2 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 97% 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) Cellular component (GO) Biological process (GO)
A (Q13526) protein bindingsearch GTPase activating protein bindingsearch isomerase activitysearch peptidyl-prolyl cis-trans isomerase activitysearch phosphoserine bindingsearch phosphothreonine bindingsearch mitogen-activated protein kinase kinase bindingsearch nucleussearch cytoplasmsearch midbodysearch nucleoplasmsearch nuclear specksearch positive regulation of ubiquitin-protein transferase activitysearch negative regulation of transforming growth factor beta receptor signaling pathwaysearch protein peptidyl-prolyl isomerizationsearch regulation of mitosissearch negative regulation of cell motilitysearch innate immune responsesearch regulation of cytokinesissearch positive regulation of Rho GTPase activitysearch protein foldingsearch negative regulation of type I interferon productionsearch cytokine-mediated signaling pathwaysearch regulation of pathway-restricted SMAD protein phosphorylationsearch negative regulation of ERK1 and ERK2 cascadesearch cell cyclesearch positive regulation of protein phosphorylationsearch

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