3kag Summary


Structure-guided design of alpha-amino acid-derived Pin1 inhibitors

The structure was published by Potter, A.J., Ray, S., Gueritz, L., et al., Murray, J.B., Richardson, C.M., and Moore, J.D., in 2010 in a paper entitled "Structure-guided design of alpha-amino acid-derived Pin1 inhibitors" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.9 Å and deposited in 2009.

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

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