1xh8 Summary

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Crystal Structures of Protein Kinase B Selective Inhibitors in Complex with Protein Kinase A and Mutants

The structure was published by Breitenlechner, C.B., Friebe, W.-G., Brunet, E., et al., Huber, R., Engh, R.A., and Masjost, B., in 2005 in a paper entitled "Design and crystal structures of protein kinase B-selective inhibitors in complex with protein kinase A and mutants" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.6 Å and deposited in 2004.

The experimental data on which the structure is based was not 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 has more than one probable quaternary state observed. For more details see the quaternary structure page.

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%
B cAMP-dependent protein kinase inhibitor, alpha form 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 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
B cAMP-dependent protein kinase inhibitorsearch

Chain ID Biological process (GO) Molecular function (GO) Cellular component (GO)
A (P00517) protein phosphorylationsearch cellular response to glucose stimulussearch positive regulation of protein export from nucleussearch positive regulation of cell cycle arrestsearch peptidyl-serine phosphorylationsearch regulation of proteasomal protein catabolic processsearch regulation of tight junction assemblysearch regulation of osteoblast differentiationsearch protein autophosphorylationsearch cellular response to parathyroid hormone stimulussearch phosphorylationsearch mesoderm formationsearch regulation of synaptic transmissionsearch sperm capacitationsearch ATP bindingsearch protein serine/threonine kinase activitysearch transferase activity, transferring phosphorus-containing groupssearch protein kinase activitysearch kinase activitysearch cAMP-dependent protein kinase activitysearch protein kinase bindingsearch transferase activitysearch ubiquitin protein ligase bindingsearch protein bindingsearch protein kinase A regulatory subunit bindingsearch nucleotide bindingsearch plasma membranesearch AMP-activated protein kinase complexsearch membranesearch nucleussearch centrosomesearch cytoplasmsearch mitochondrionsearch sperm midpiecesearch 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
B cAMP-dependent protein kinase inhibitorsearch