2c1b Summary

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STRUCTURE OF CAMP-DEPENDENT PROTEIN KINASE COMPLEXED WITH (4R,2S)-5'-(4-(4-CHLOROBENZYLOXY)PYRROLIDIN-2-YLMETHANESULFONYL)ISOQUINOLINE

The structure was published by Collins, I., Caldwell, J., Fonseca, T., et al., Wyatt, P.G., Workman, P., and Mcdonald, E., in 2006 in a paper entitled "Structure-Based Design of Isoquinoline-5-Sulfonamide Inhibitors of Protein Kinase B." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 2005.

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 and CAMP-DEPENDENT PROTEIN KINASE INHIBITOR.

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 P00517 (2-351) (KAPCA_BOVIN)search Bos taurussearch 96% 351 96%
I CAMP-DEPENDENT PROTEIN KINASE INHIBITOR P61925 (6-25) (IPKA_HUMAN)search Homo sapienssearch < 90% 20 100%


This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
P00517 (2 - 351) CAMP-DEPENDENT PROTEIN KINASE Bos taurus
P61925 (6 - 25) CAMP-DEPENDENT PROTEIN KINASE INHIBITOR HOMO SAPIENS

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 cAMP-dependent protein kinase inhibitorsearch

Chain ID Cellular component (GO) Biological process (GO) Molecular function (GO)
A (P00517) plasma membranesearch cytoplasmsearch nucleussearch neuromuscular junctionsearch sperm midpiecesearch ciliary basesearch membranesearch AMP-activated protein kinase complexsearch extracellular vesicular exosomesearch mitochondrionsearch centrosomesearch cellular response to parathyroid hormone stimulussearch regulation of osteoblast differentiationsearch peptidyl-serine phosphorylationsearch negative regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterningsearch sperm capacitationsearch protein phosphorylationsearch phosphorylationsearch regulation of proteasomal protein catabolic processsearch regulation of synaptic transmissionsearch regulation of protein processingsearch positive regulation of cell cycle arrestsearch protein autophosphorylationsearch cellular response to glucose stimulussearch regulation of tight junction assemblysearch positive regulation of protein export from nucleussearch neural tube closuresearch peptidyl-threonine phosphorylationsearch mesoderm formationsearch transferase activitysearch cAMP-dependent protein kinase activitysearch nucleotide bindingsearch ATP bindingsearch protein kinase activitysearch protein serine/threonine kinase activitysearch protein serine/threonine/tyrosine kinase activitysearch protein kinase bindingsearch ubiquitin protein ligase bindingsearch kinase activitysearch protein kinase A regulatory subunit bindingsearch protein bindingsearch transferase activity, transferring phosphorus-containing groupssearch
I (P61925) negative regulation of protein kinase activitysearch cAMP-dependent protein kinase inhibitor activitysearch

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