2xp3 Summary

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DISCOVERY OF CELL-ACTIVE PHENYL-IMIDAZOLE PIN1 INHIBITORS BY STRUCTURE-GUIDED FRAGMENT EVOLUTION

The structure was published by Potter, A., Oldfield, V., Nunns, C., et al., Richardson, C.M., Murray, J.B., and Moore, J.D., in 2010 in a paper entitled "Discovery of Cell-Active Phenyl-Imidazole Pin1 Inhibitors by Structure-Guided Fragment Evolution." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 2010.

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 167 residues which is 100% of the natural sequence. Out of 167 residues 145 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% 167 86%


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

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