2gnj Summary


PKA three fold mutant model of Rho-kinase with Y-27632

The structure was published by Bonn, S., Herrero, S., Breitenlechner, C.B., et al., Engh, R.A., Gassel, M., and Bossemeyer, D., in 2006 in a paper entitled "Structural analysis of protein kinase A mutants with Rho-kinase inhibitor specificity" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.28 Å and deposited in 2006.

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.

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 Q3SX13 (6-25) (IPKA_BOVIN)search Bos taurussearch < 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
Q3SX13 (6 - 25) cAMP-dependent protein kinase inhibitor alpha

Chain Structural classification (CATH) Sequence family (Pfam)
A (P00517) Transferase(Phosphotransferase) domain 1search, Phosphorylase Kinase; domain 1search PF00069: Protein kinase domainsearch
I cAMP-dependent protein kinase inhibitorsearch

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

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