1q62 Summary


PKA double mutant model of PKB

The structure was published by Gassel, M., Breitenlechner, C.B., Rueger, P., et al., Huber, R., Bossemeyer, D., and Engh, R.A., in 2003 in a paper entitled "Mutants of protein kinase A that mimic the ATP-binding site of protein kinase B (AKT)" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.3 Å and deposited in 2003.

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 cAMP-dependent protein kinase inhibitor, alpha form.

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 P00517 (2-351) (KAPCA_BOVIN)search Bos taurussearch 96% 350 96%
I cAMP-dependent protein kinase inhibitor, alpha form P61925 (6-25) (IPKA_HUMAN)search Homo sapienssearch 100% 20 100%

This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
P00517 (2 - 351) cAMP-dependent protein kinase, alpha-catalytic subunit Bos taurus
P61925 (6 - 25) cAMP-dependent protein kinase inhibitor, alpha form

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 (P61925) PF02827: cAMP-dependent protein kinase inhibitorsearch

Chain ID Molecular function (GO) Cellular component (GO) Biological process (GO)
A (P00517) protein kinase activitysearch transferase activity, transferring phosphorus-containing groupssearch ATP bindingsearch protein kinase A regulatory subunit bindingsearch protein bindingsearch protein serine/threonine kinase activitysearch protein serine/threonine/tyrosine kinase activitysearch cAMP-dependent protein kinase activitysearch transferase activitysearch nucleotide bindingsearch kinase activitysearch protein kinase bindingsearch ubiquitin protein ligase bindingsearch ciliary basesearch neuromuscular junctionsearch mitochondrionsearch membranesearch centrosomesearch AMP-activated protein kinase complexsearch cytoplasmsearch nucleussearch plasma membranesearch extracellular exosomesearch sperm midpiecesearch regulation of osteoblast differentiationsearch sperm capacitationsearch cellular response to parathyroid hormone stimulussearch protein autophosphorylationsearch mesoderm formationsearch regulation of protein processingsearch positive regulation of protein export from nucleussearch peptidyl-serine phosphorylationsearch cellular response to glucose stimulussearch regulation of proteasomal protein catabolic processsearch peptidyl-threonine phosphorylationsearch regulation of tight junction assemblysearch neural tube closuresearch positive regulation of cell cycle arrestsearch regulation of synaptic transmissionsearch negative regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterningsearch protein phosphorylationsearch phosphorylationsearch

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