2gni Summary


PKA fivefold mutant model of Rho-kinase with inhibitor Fasudil (HA1077)

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

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