3CQW: Akt-1

Crystal Structure of Akt-1 complexed with substrate peptide and inhibitor. Determined by X-ray diffraction at 2.0 Å resolution. Released 27 May 2008.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,926
Mol. weight: 41.06 kDa
Ligands: CQW, MN
Released: 27 May 2008

Explore 3CQW in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3CQW contains 20 α-helices and 16 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 19 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	147-149	3
β-strand	150-158	9	1
β-strand	162-169	8	1
β-strand	175-182	8	1
α-helix	183-188	6
α-helix	192-204	13
β-strand	210	1	2
β-strand	213-218	6	1
β-strand	222-227	6	1
β-strand	234	1	2
α-helix	235-242	8
α-helix	247-266	20
β-strand	271	1	3
α-helix	277-279	3
β-strand	280-282	3	2
β-strand	288-290	3	2
α-helix	296	1
β-strand	297	1	3
α-helix	298	1
β-strand	306	1	4
β-strand	310-311	2	5
α-helix	313-315	3
α-helix	318-321	4
β-strand	326	1	4
α-helix	330-344	15
α-helix	354-363	10
α-helix	364-367	4
α-helix	374-383	10
α-helix	388-390	3
α-helix	399-403	5
α-helix	406-408	3
α-helix	413-417	5
α-helix	440-443	4
β-strand	474-475	2	1

Chain C: 1 helix, 1 β-strand

Element	Residues	Length	Sheet
α-helix	2-5	4
β-strand	8-9	2	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
RAC-alpha serine/threonine-protein kinase	A	protein	342	Homo sapiens	P31749 (AlphaFold model)
Glycogen synthase kinase-3 beta	C	protein	10	Homo sapiens	P49841 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3CQW_1 RAC-alpha serine/threonine-protein kinase (chains A)
GAMDPRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTE
NRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIV
SALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAP
EVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKS
LLSGLLKKDPKQRLGGGSEDAKEIMQHRFFAGIVWQHVYEKKLSPPFKPQVTSETDTRYF
DEEFTAQMITITPPDQDDSMECVDSERRPHFPQFDYSASSTA

Sequence of entity 2 (C), FASTA

>3CQW_2 Glycogen synthase kinase-3 beta (chains C)
GRPRTTSFAE

Ligands and cofactors

ID	Name	Formula	Copies
CQW	5-(5-chloro-7H-pyrrolo[2,3-d]pyrimidin-4-yl)-4,5,6,7-tetrahydro-1H-imidazo[4,5-…	C12 H11 Cl N6	1
MN	Manganese (II) ion	Mn	1

Primary citation

Synthesis and structure based optimization of novel Akt inhibitors. Lippa, B., Pan, G., Corbett, M. et al. Bioorg Med Chem Lett (2008) 18:3359-3363. DOI 10.1016/j.bmcl.2008.04.034 · PubMed

Other PDB entries of the same protein (UniProt P31749 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1UNQ 0.98 Å, High resolution crystal structure of the Pleckstrin Homology Domain Of Protein Kinase…
1UNR 1.25 Å, Crystal structure of the PH domain of PKB alpha in complex with a sulfate molecule
7MYX 1.39 Å, Crystal structure of the PH domain (R86A) of Akt1
1H10 1.4 Å, High resolution structure of the pleckstrin homology domain of protein kinase b/akt…
8JOW 1.4 Å, Crystal structure of rabbit antibody with phosphorylated peptide bound
4GV1 1.49 Å, PKB alpha in complex with AZD5363
1UNP 1.65 Å, Crystal structure of the pleckstrin homology domain of PKB alpha
3QKL 1.9 Å, Spirochromane Akt Inhibitors
7NH5 1.9 Å, Co-Crystal Structure of Akt1 in Complex with Covalent-Allosteric Akt Inhibitor 6
8UW9 1.9 Å, Structure of AKT1(E17K) with compound 4
9TMV 1.9 Å, Akt1 mutant in complex with the 3-ethyl 1-methyl 1,4-substituted pyrazole containing…
2UVM 1.94 Å, Structure of PKBalpha PH domain in complex with a novel inositol headgroup surrogate,…

Browse structure collections

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