3tdb Summary


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 Sequence family (Pfam)
A (Q13526) PF00397: WW domainsearch, PF00639: PPIC-type PPIASE domainsearch

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