2q5a Summary


PDB entry 2q5a (supersedes 2iti)

human Pin1 bound to L-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 1.5 Å and deposited in 2007.

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 Five residue 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 96% 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 GTPase activating protein bindingsearch protein bindingsearch phosphothreonine bindingsearch peptidyl-prolyl cis-trans isomerase activitysearch phosphoserine bindingsearch mitogen-activated protein kinase kinase bindingsearch midbodysearch nuclear specksearch nucleussearch nucleoplasmsearch cytoplasmsearch cytokine-mediated signaling pathwaysearch regulation of cytokinesissearch positive regulation of ubiquitin-protein transferase activitysearch regulation of pathway-restricted SMAD protein phosphorylationsearch regulation of mitotic nuclear divisionsearch protein peptidyl-prolyl isomerizationsearch metabolic processsearch negative regulation of ERK1 and ERK2 cascadesearch negative regulation of type I interferon productionsearch innate immune responsesearch positive regulation of protein phosphorylationsearch positive regulation of GTPase activitysearch negative regulation of transforming growth factor beta receptor signaling pathwaysearch cell cyclesearch negative regulation of cell motilitysearch

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