1ydt Summary

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STRUCTURE OF CAMP-DEPENDENT PROTEIN KINASE, ALPHA-CATALYTIC SUBUNIT IN COMPLEX WITH H89 PROTEIN KINASE INHIBITOR N-[2-(4-BROMOCINNAMYLAMINO)ETHYL]-5-ISOQUINOLINE

The structure was published by Engh, R.A., Girod, A., Kinzel, V., Huber, R., and Bossemeyer, D., in 1996 in a paper entitled "Crystal structures of catalytic subunit of cAMP-dependent protein kinase in complex with isoquinolinesulfonyl protein kinase inhibitors H7, H8, and H89. Structural implications for selectivity." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.3 Å and deposited in 1996.

The experimental data on which the structure is based was also deposited.

This PDB entry contains a complex of 2 biomacromolecules, namely C-AMP-DEPENDENT PROTEIN KINASE and PROTEIN KINASE INHIBITOR PEPTIDE.

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
E C-AMP-DEPENDENT PROTEIN KINASE P00517 (2-351) (KAPCA_BOVIN)search Bos taurussearch 96% 350 96%
I PROTEIN KINASE INHIBITOR PEPTIDE P63249 (6-25) (IPKA_RAT)search Rattus norvegicussearch < 90% 20 100%


This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
P00517 (2 - 351) C-AMP-DEPENDENT PROTEIN KINASE Bos taurus
P63249 (6 - 25) PROTEIN KINASE INHIBITOR PEPTIDE

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

Chain InterPro annotation
E 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