2itk Summary


human Pin1 bound to D-PEPTIDE

The structure was published by Zhang, Y., Daum, S., Wildemann, D., et al., Lu, K.P., Fischer, G., and Noel, J.P., in 2007 in a paper entitled "Structural basis for high-affinity peptide inhibition of human Pin1." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.45 Å and deposited in 2006.

The experimental data on which the structure is based was also deposited.

This PDB entry contains a complex of 2 biomacromolecules, namely Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 and D-Peptide.

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 most likely forms heterodimers.

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 (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (Q13526) WW domainsearch, FKBP immunophilin/proline isomerasesearch Ubiquitin Ligase Nedd4; Chain: W;search, Chitinase A; domain 3search PF00397: WW domainsearch, PF00639: PPIC-type PPIASE domainsearch

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

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