1f8a Summary

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STRUCTURAL BASIS FOR THE PHOSPHOSERINE-PROLINE RECOGNITION BY GROUP IV WW DOMAINS

The structure was published by Verdecia, M.A., Bowman, M.E., Lu, K.P., Hunter, T., and Noel, J.P., in 2000 in a paper entitled "Structural basis for phosphoserine-proline recognition by group IV WW domains." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.84 Å and deposited in 2000.

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 Y(SEP)PT(SEP)S PEPTIDE.

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
B PEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 1 Q13526 (1-163) (PIN1_HUMAN)search Homo sapienssearch 97% 167 92%
C Y(SEP)PT(SEP)S PEPTIDE Not available
Synthetic Not available 7 100%


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)
B (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
C

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

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