3e8d Summary

pdbe.org/3e8d
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Crystal structures of the kinase domain of AKT2 in complex with ATP-competitive inhibitors

The structure was published by Rouse, M.B., Seefeld, M.A., Leber, J.D., et al., Choudhry, A.E., Schaber, M.D., and Heerding, D.A., in 2009 in a paper entitled "Aminofurazans as potent inhibitors of AKT kinase" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.7 Å and deposited in 2008.

The experimental data on which the structure is based was also deposited.

This PDB entry contains a complex of 2 biomacromolecules, namely RAC-beta serine/threonine-protein kinase and Glycogen synthase kinase-3 beta peptide.

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 RAC-beta serine/threonine-protein kinase P31751 (146-480) (AKT2_HUMAN)search Homo sapienssearch < 90% 335 94%
B RAC-beta serine/threonine-protein kinase P31751 (146-480) (AKT2_HUMAN)search Homo sapienssearch < 90% 335 94%
C Glycogen synthase kinase-3 beta peptide P49841 (3-12) (GSK3B_HUMAN)search Homo sapienssearch 91% 10 100%
D Glycogen synthase kinase-3 beta peptide P49841 (3-12) (GSK3B_HUMAN)search Homo sapienssearch 91% 10 100%


This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
P31751 (146 - 480) RAC-beta serine/threonine-protein kinase Homo sapiens
P49841 (3 - 12) Glycogen synthase kinase-3 beta peptide

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B Protein kinases, catalytic subunitsearch Phosphorylase Kinase; domain 1search, Transferase(Phosphotransferase) domain 1search Protein kinase domainsearch, Protein kinase C terminal domainsearch
C, D (P49841)

Chain ID Molecular function (GO) Biological process (GO)
A, B (P31751) protein kinase activitysearch ATP bindingsearch protein serine/threonine kinase activitysearch transferase activity, transferring phosphorus-containing groupssearch protein phosphorylationsearch

Chain InterPro annotation
A, B 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 Protein kinase, C-terminalsearch
C, D