1syk Summary

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

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