2uw6 Summary

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STRUCTURE OF PKA-PKB CHIMERA COMPLEXED WITH (S)-2-(4-CHLORO-PHENYL)-2-(4-1H-PYRAZOL-4-YL)-PHENYL)-ETHYLAMINE

The structure was published by Saxty, G., Woodhead, S.J., Berdini, V., et al., Downham, R., Garrett, M.D., and Carr, R.A., in 2007 in a paper entitled "Identification of Inhibitors of Protein Kinase B Using Fragment-Based Lead Discovery" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.23 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 CAMP-DEPENDENT PROTEIN KINASE, ALPHA-CATALYTIC SUBUNIT and CAMP-DEPENDENT PROTEIN KINASE INHIBITOR ALPHA.

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 CAMP-DEPENDENT PROTEIN KINASE, ALPHA-CATALYTIC SUBUNIT P00517 (2-351) (KAPCA_BOVIN)search Bos taurussearch 96% 351 96%
I CAMP-DEPENDENT PROTEIN KINASE INHIBITOR ALPHA P61925 (6-25) (IPKA_HUMAN)search Homo sapienssearch < 90% 20 100%


This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
P00517 (2 - 351) CAMP-DEPENDENT PROTEIN KINASE, ALPHA-CATALYTIC SUBUNIT Bos taurus
P61925 (6 - 25) CAMP-DEPENDENT PROTEIN KINASE INHIBITOR ALPHA HOMO SAPIENS

Chain Structural classification (CATH) Sequence family (Pfam)
A (P00517) Transferase(Phosphotransferase) domain 1search, Phosphorylase Kinase; domain 1search PF00069: Protein kinase domainsearch
I cAMP-dependent protein kinase inhibitorsearch

Chain ID Molecular function (GO) Cellular component (GO) Biological process (GO)
A (P00517) ATP bindingsearch cAMP-dependent protein kinase activitysearch transferase activitysearch protein kinase activitysearch transferase activity, transferring phosphorus-containing groupssearch protein serine/threonine kinase activitysearch protein kinase bindingsearch kinase activitysearch protein serine/threonine/tyrosine kinase activitysearch protein bindingsearch nucleotide bindingsearch protein kinase A regulatory subunit bindingsearch ubiquitin protein ligase bindingsearch centrosomesearch plasma membranesearch nucleussearch membranesearch cytoplasmsearch ciliary basesearch neuromuscular junctionsearch mitochondrionsearch AMP-activated protein kinase complexsearch extracellular vesicular exosomesearch sperm midpiecesearch peptidyl-serine phosphorylationsearch peptidyl-threonine phosphorylationsearch protein phosphorylationsearch mesoderm formationsearch phosphorylationsearch regulation of osteoblast differentiationsearch neural tube closuresearch negative regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterningsearch sperm capacitationsearch positive regulation of protein export from nucleussearch cellular response to parathyroid hormone stimulussearch positive regulation of cell cycle arrestsearch cellular response to glucose stimulussearch regulation of synaptic transmissionsearch protein autophosphorylationsearch regulation of protein processingsearch regulation of tight junction assemblysearch regulation of proteasomal protein catabolic processsearch
I (P61925) cAMP-dependent protein kinase inhibitor activitysearch negative regulation of protein kinase activitysearch

Chain InterPro annotation
A Protein kinase domainsearch AGC-kinase, C-terminalsearch Serine/threonine/dual specificity protein kinase, catalytic domainsearch Serine/threonine-protein kinase, active sitesearch Protein kinase-like domainsearch Protein kinase, ATP binding sitesearch
I cAMP-dependent protein kinase inhibitorsearch