3idc Summary

pdbe.org/3idc
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Crystal structure of (102-265)RIIb:C holoenzyme of cAMP-dependent protein kinase

The structure was published by Brown, S.H., Wu, J., Kim, C., Alberto, K., and Taylor, S.S., in 2009 in a paper entitled "Novel isoform-specific interfaces revealed by PKA RIIbeta holoenzyme structures." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.7 Å and deposited in 2009.

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 catalytic subunit alpha and cAMP-dependent protein kinase type II-beta regulatory subunit.

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 catalytic subunit alpha P05132 (2-351) (KAPCA_MOUSE)search Mus musculussearch 96% 350 98%
B cAMP-dependent protein kinase type II-beta regulatory subunit P12369 (102-265) (KAP3_RAT)search Rattus norvegicussearch < 90% 164 97%


This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
P05132 (2 - 351) cAMP-dependent protein kinase catalytic subunit alpha Mus musculus
P12369 (102 - 265) cAMP-dependent protein kinase type II-beta regulatory subunit Rattus norvegicus

Chain Structural classification (CATH) Sequence family (Pfam)
A (P05132) Transferase(Phosphotransferase) domain 1search, Phosphorylase Kinase; domain 1search PF00069: Protein kinase domainsearch
B Jelly Rollssearch Cyclic nucleotide-binding domainsearch

Chain ID Cellular component (GO) Biological process (GO) Molecular function (GO)
A (P05132) cytoplasmsearch sperm midpiecesearch AMP-activated protein kinase complexsearch plasma membranesearch membranesearch nucleussearch ciliary basesearch nucleoplasmsearch cytosolsearch ciliumsearch centrosomesearch neuromuscular junctionsearch mitochondrionsearch cell projectionsearch regulation of proteasomal protein catabolic processsearch peptidyl-serine phosphorylationsearch protein autophosphorylationsearch phosphorylationsearch sperm capacitationsearch cellular response to glucose stimulussearch regulation of synaptic transmissionsearch regulation of tight junction assemblysearch positive regulation of cell cycle arrestsearch protein phosphorylationsearch mesoderm formationsearch negative regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterningsearch neural tube closuresearch regulation of osteoblast differentiationsearch regulation of protein processingsearch cellular response to parathyroid hormone stimulussearch peptidyl-threonine phosphorylationsearch positive regulation of protein export from nucleussearch protein kinase activitysearch protein bindingsearch ATP bindingsearch cAMP-dependent protein kinase activitysearch ubiquitin protein ligase bindingsearch protein serine/threonine/tyrosine kinase activitysearch protein serine/threonine kinase activitysearch kinase activitysearch nucleotide bindingsearch transferase activitysearch protein kinase bindingsearch protein kinase A regulatory subunit bindingsearch

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
B Cyclic nucleotide-binding domainsearch cAMP/cGMP-dependent protein kinasesearch RmlC-like jelly roll foldsearch Cyclic nucleotide-binding, conserved sitesearch Cyclic nucleotide-binding-likesearch