2jds Summary



The structure was published by Davies, T.G., Verdonk, M.L., Graham, B., et al., Woodhead, S.J., Jhoti, H., and Barford, D., in 2007 in a paper entitled "A Structural Comparison of Inhibitor Binding to Pkb, Pka and Pka-Pkb Chimera" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.0 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 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 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 Bos taurus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P00517) Protein kinases, catalytic subunitsearch 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 protein kinase A regulatory subunit bindingsearch protein kinase activitysearch protein serine/threonine kinase activitysearch transferase activity, transferring phosphorus-containing groupssearch transferase activitysearch protein bindingsearch kinase activitysearch protein kinase bindingsearch ubiquitin protein ligase bindingsearch nucleotide bindingsearch protein serine/threonine/tyrosine kinase activitysearch cytoplasmsearch membranesearch mitochondrionsearch neuromuscular junctionsearch nucleussearch AMP-activated protein kinase complexsearch plasma membranesearch extracellular vesicular exosomesearch sperm midpiecesearch ciliary basesearch centrosomesearch cellular response to parathyroid hormone stimulussearch regulation of proteasomal protein catabolic processsearch regulation of osteoblast differentiationsearch positive regulation of protein export from nucleussearch negative regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterningsearch protein phosphorylationsearch peptidyl-threonine phosphorylationsearch neural tube closuresearch regulation of protein processingsearch peptidyl-serine phosphorylationsearch mesoderm formationsearch phosphorylationsearch regulation of synaptic transmissionsearch protein autophosphorylationsearch sperm capacitationsearch cellular response to glucose stimulussearch regulation of tight junction assemblysearch positive regulation of cell cycle arrestsearch
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