3tdb Summary

pdbe.org/3tdb
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Human Pin1 bound to trans peptidomimetic inhibitor

The structure was published by Zhang, M., Wang, X.J., Chen, X., et al., Ellington, A.D., Etzkorn, F.A., and Zhang, Y., in 2012 in a paper entitled "Structural and Kinetic Analysis of Prolyl-isomerization/Phosphorylation Cross-Talk in the CTD Code." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.267 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 1. This molecule has the UniProt identifier Q13526 (PIN1_HUMAN)search. The sample contained 158 residues which is 97% of the natural sequence. Out of 158 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 (6-163) (PIN1_HUMAN)search Homo sapienssearch 97% 158 92%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q13526 (6 - 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 phosphoserine bindingsearch GTPase activating protein bindingsearch peptidyl-prolyl cis-trans isomerase activitysearch isomerase activitysearch phosphothreonine bindingsearch mitogen-activated protein kinase kinase bindingsearch regulation of pathway-restricted SMAD protein phosphorylationsearch negative regulation of cell motilitysearch negative regulation of type I interferon productionsearch regulation of cytokinesissearch metabolic processsearch cytokine-mediated signaling pathwaysearch cell cyclesearch positive regulation of protein phosphorylationsearch positive regulation of Rho GTPase activitysearch positive regulation of ubiquitin-protein transferase activitysearch negative regulation of transforming growth factor beta receptor signaling pathwaysearch regulation of mitosissearch protein peptidyl-prolyl isomerizationsearch negative regulation of ERK1 and ERK2 cascadesearch innate immune responsesearch nucleussearch nucleoplasmsearch midbodysearch cytoplasmsearch nuclear specksearch

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