1rek Summary

pdbe.org/1rek
spacer

Crystal structure of cAMP-dependent protein kinase complexed with balanol analog 8

The structure was published by Akamine, P., Madhusudan, Brunton, L.L., et al., Canaves, J.M., Xuong, N.H., and Taylor, S.S., in 2004 in a paper entitled "Balanol analogues probe specificity determinants and the conformational malleability of the cyclic 3',5'-adenosine monophosphate-dependent protein kinase catalytic subunit" (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 not deposited.

The PDB entry contains the structure of cAMP-dependent protein kinase, alpha-catalytic subunit. 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 323 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, alpha-catalytic subunit 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, alpha-catalytic subunit 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) Molecular function (GO) Cellular component (GO)
A (P05132) protein phosphorylationsearch peptidyl-serine phosphorylationsearch negative regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterningsearch neural tube closuresearch peptidyl-threonine phosphorylationsearch sperm capacitationsearch positive regulation of protein export from nucleussearch positive regulation of cell cycle arrestsearch regulation of proteasomal protein catabolic processsearch phosphorylationsearch regulation of synaptic transmissionsearch regulation of protein processingsearch cellular response to parathyroid hormone stimulussearch cellular response to glucose stimulussearch regulation of osteoblast differentiationsearch regulation of tight junction assemblysearch protein autophosphorylationsearch mesoderm formationsearch protein kinase activitysearch protein serine/threonine kinase activitysearch ATP bindingsearch protein bindingsearch cAMP-dependent protein kinase activitysearch kinase activitysearch protein kinase bindingsearch ubiquitin protein ligase bindingsearch protein serine/threonine/tyrosine kinase activitysearch transferase activitysearch nucleotide bindingsearch protein kinase A regulatory subunit bindingsearch transferase activity, transferring phosphorus-containing groupssearch nucleussearch cytosolsearch plasma membranesearch mitochondrionsearch ciliary basesearch cell projectionsearch extracellular vesicular exosomesearch membranesearch cytoplasmsearch centrosomesearch neuromuscular junctionsearch motile ciliumsearch AMP-activated protein kinase complexsearch sperm midpiecesearch nucleoplasmsearch ciliumsearch

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