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) Biological process (GO) Cellular component (GO)
A (P00517) ATP bindingsearch protein serine/threonine kinase activitysearch transferase activity, transferring phosphorus-containing groupssearch protein kinase activitysearch kinase activitysearch nucleotide bindingsearch protein kinase bindingsearch transferase activitysearch cAMP-dependent protein kinase activitysearch protein bindingsearch ubiquitin protein ligase bindingsearch protein kinase A regulatory subunit bindingsearch protein phosphorylationsearch regulation of osteoblast differentiationsearch positive regulation of protein export from nucleussearch protein autophosphorylationsearch regulation of tight junction assemblysearch positive regulation of cell cycle arrestsearch mesoderm formationsearch cellular response to glucose stimulussearch phosphorylationsearch regulation of proteasomal protein catabolic processsearch sperm capacitationsearch regulation of synaptic transmissionsearch peptidyl-serine phosphorylationsearch cellular response to parathyroid hormone stimulussearch mitochondrionsearch nucleussearch neuromuscular junctionsearch membranesearch sperm midpiecesearch plasma membranesearch cytoplasmsearch AMP-activated protein kinase complexsearch centrosomesearch

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