1q24 Summary

pdbe.org/1q24
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PKA double mutant model of PKB in complex with MgATP

The structure was published by Gassel, M., Breitenlechner, C.B., Rueger, P., et al., Huber, R., Bossemeyer, D., and Engh, R.A., in 2003 in a paper entitled "Mutants of protein kinase A that mimic the ATP-binding site of protein kinase B (AKT)" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.6 Å and deposited in 2003.

The experimental data on which the structure is based was also 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 96%
I cAMP-dependent Protein Kinase Inhibitor, alpha form Q71U53 (6-25) (IPKA_PIG)search Sus scrofasearch < 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
Q71U53 (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
I cAMP-dependent protein kinase inhibitorsearch

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

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