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

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