1bx6 Summary



The structure was published by Narayana, N., Diller, T.C., Koide, K., et al., Xuong, N.H., Ten Eyck, L.F., and Taylor, S.S., in 1999 in a paper entitled "Crystal structure of the potent natural product inhibitor balanol in complex with the catalytic subunit of cAMP-dependent protein kinase." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.1 Å and deposited in 1998.

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

The PDB entry contains the structure of CAMP-DEPENDENT PROTEIN KINASE. This molecule has the UniProt identifier P05132 (KAPCA_MOUSE)search. The sample contained 350 residues which is 100% of the natural sequence. Out of 350 residues 339 were observed and are deposited in the PDB.

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 is most likely monomeric.

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 P05132 (2-351) (KAPCA_MOUSE)search Mus musculussearch 96% 350 96%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P05132 (2 - 351) CAMP-DEPENDENT PROTEIN KINASE Mus musculus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P05132) Protein kinases, catalytic subunitsearch Transferase(Phosphotransferase) domain 1search, Phosphorylase Kinase; domain 1search PF00069: Protein kinase domainsearch

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

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