1syk Summary


Crystal structure of E230Q mutant of cAMP-dependent protein kinase reveals unexpected apoenzyme conformation

The structure was published by Wu, J., Yang, J., Kannan, N., et al., Xuong, N.H., Ten Eyck, L.F., and Taylor, S.S., in 2005 in a paper entitled "Crystal structure of the E230Q mutant of cAMP-dependent protein kinase reveals an unexpected apoenzyme conformation and an extended N-terminal A helix." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.8 Å and deposited in 2004.

The experimental data on which the structure is based was also deposited.

This PDB entry contains multiple copies of the structure of cAMP-dependent protein kinase, alpha-catalytic subunit.

The molecule has more than one probable quaternary state observed. For more details see the quaternary structure page.

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% 350 100%
B cAMP-dependent protein kinase, alpha-catalytic subunit P05132 (2-351) (KAPCA_MOUSE)search Mus musculussearch 96% 350 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P05132 (2 - 351) cAMP-dependent protein kinase, alpha-catalytic subunit Mus musculus

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

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

Chain InterPro annotation
A, B 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