2qur Summary

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Crystal Structure of F327A/K285P Mutant of cAMP-dependent Protein Kinase

The structure was published by Yang, J., Kennedy, E.J., Wu, J., et al., Pennypacker, J., Ghosh, G., and Taylor, S.S., in 2009 in a paper entitled "Contribution of non-catalytic core residues to activity and regulation in protein kinase A." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.5 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 cAMP-dependent protein kinase, alpha-catalytic subunit and 20-mer fragment from 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 P05132 (2-351) (KAPCA_MOUSE)search Mus musculussearch 96% 350 97%
B 20-mer fragment from cAMP-dependent protein kinase inhibitor alpha P63248 (6-25) (IPKA_MOUSE)search Mus musculussearch < 90% 20 100%


This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
P05132 (2 - 351) cAMP-dependent protein kinase, alpha-catalytic subunit Mus musculus
P63248 (6 - 25) 20-mer fragment from cAMP-dependent protein kinase inhibitor alpha

Chain Structural classification (CATH) Sequence family (Pfam)
A (P05132) Transferase(Phosphotransferase) domain 1search, Phosphorylase Kinase; domain 1search PF00069: Protein kinase domainsearch
B cAMP-dependent protein kinase inhibitorsearch

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

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 cAMP-dependent protein kinase inhibitorsearch