1atp Summary


2.2 angstrom refined crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MNATP and a peptide inhibitor

The structure was published by Zheng, J., Trafny, E.A., Knighton, D.R., et al., Taylor, S.S., Ten Eyck, L.F., and Sowadski, J.M., in 1993 in a paper entitled "2.2 A refined crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MnATP and a peptide inhibitor." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.2 Å and deposited in 1993.

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 and PEPTIDE INHIBITOR PKI(5-24).

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
E cAMP-DEPENDENT PROTEIN KINASE P05132 (2-351) (KAPCA_MOUSE)search Mus musculussearch 96% 350 96%
I PEPTIDE INHIBITOR PKI(5-24) P63248 (6-25) (IPKA_MOUSE)search Mus musculussearch < 90% 20 100%

This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
P05132 (2 - 351) cAMP-DEPENDENT PROTEIN KINASE Mus musculus
P63248 (6 - 25) PEPTIDE INHIBITOR PKI(5-24) Mus musculus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
E (P05132) Protein kinases, catalytic subunitsearch 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)
E (P05132) protein phosphorylationsearch positive regulation of cell cycle arrestsearch cellular response to glucose stimulussearch sperm capacitationsearch positive regulation of protein export from nucleussearch regulation of protein processingsearch cellular response to parathyroid hormone stimulussearch phosphorylationsearch regulation of tight junction assemblysearch peptidyl-serine phosphorylationsearch neural tube closuresearch regulation of osteoblast differentiationsearch regulation of proteasomal protein catabolic processsearch peptidyl-threonine phosphorylationsearch mesoderm formationsearch protein autophosphorylationsearch regulation of synaptic transmissionsearch negative regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterningsearch transferase activity, transferring phosphorus-containing groupssearch protein kinase activitysearch ATP bindingsearch protein serine/threonine kinase activitysearch protein kinase A regulatory subunit bindingsearch kinase activitysearch protein bindingsearch protein serine/threonine/tyrosine kinase activitysearch protein kinase bindingsearch nucleotide bindingsearch transferase activitysearch ubiquitin protein ligase bindingsearch cAMP-dependent protein kinase activitysearch membranesearch cytoplasmsearch sperm midpiecesearch cytosolsearch neuromuscular junctionsearch nucleussearch AMP-activated protein kinase complexsearch centrosomesearch ciliumsearch ciliary basesearch mitochondrionsearch plasma membranesearch nucleoplasmsearch motile ciliumsearch extracellular vesicular exosomesearch cell projectionsearch
I (P63248) negative regulation of protein kinase activitysearch cAMP-dependent protein kinase inhibitor activitysearch

Chain InterPro annotation
E 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