1sve Summary

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Crystal Structure of Protein Kinase A in Complex with Azepane Derivative 1

The structure was published by Breitenlechner, C.B., Wegge, T., Berillon, L., et al., Huber, R., Engh, R.A., and Masjost, B., in 2004 in a paper entitled "Structure-based optimization of novel azepane derivatives as PKB inhibitors" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.49 Å and deposited in 2004.

The experimental data on which the structure is based was not 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.

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 P00517 (2-351) (KAPCA_BOVIN)search Bos taurussearch 96% 350 98%
B cAMP-dependent protein kinase inhibitor, alpha form P61926 (6-25) (IPKA_RABIT)search Oryctolagus cuniculussearch < 90% 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
P61926 (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
B cAMP-dependent protein kinase inhibitorsearch

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