2gnh Summary


PKA five fold mutant model of Rho-kinase with H1152P

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 2.05 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 97%
I cAMP-dependent protein kinase inhibitor alpha P61926 (6-25) (IPKA_RABIT)search Oryctolagus cuniculussearch < 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
P61926 (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 Molecular function (GO) Cellular component (GO) Biological process (GO)
A (P00517) cAMP-dependent protein kinase activitysearch protein kinase activitysearch protein serine/threonine/tyrosine kinase activitysearch protein serine/threonine kinase activitysearch ATP bindingsearch transferase activity, transferring phosphorus-containing groupssearch protein kinase bindingsearch protein kinase A regulatory subunit bindingsearch ubiquitin protein ligase bindingsearch transferase activitysearch protein bindingsearch nucleotide bindingsearch kinase activitysearch centrosomesearch AMP-activated protein kinase complexsearch ciliary basesearch cytoplasmsearch membranesearch mitochondrionsearch nucleussearch sperm midpiecesearch plasma membranesearch extracellular vesicular exosomesearch neuromuscular junctionsearch sperm capacitationsearch positive regulation of cell cycle arrestsearch phosphorylationsearch mesoderm formationsearch regulation of osteoblast differentiationsearch regulation of tight junction assemblysearch cellular response to glucose stimulussearch regulation of proteasomal protein catabolic processsearch protein phosphorylationsearch peptidyl-serine phosphorylationsearch positive regulation of protein export from nucleussearch regulation of synaptic transmissionsearch neural tube closuresearch negative regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterningsearch protein autophosphorylationsearch peptidyl-threonine phosphorylationsearch cellular response to parathyroid hormone stimulussearch regulation of protein processingsearch

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