3QKL: Spirochromane Akt Inhibitors

Spirochromane Akt Inhibitors. Determined by X-ray diffraction at 1.9 Å resolution. Released 30 Mar 2011.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,959
Mol. weight: 41.15 kDa
Ligands: SMR
Released: 30 Mar 2011

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

Secondary structure: helices and β-sheets

3QKL 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: 20 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	147-149	3
β-strand	150-159	10	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	222-228	7	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	399-403	5
α-helix	406-408	3
α-helix	413-417	5
α-helix	422-423	2
α-helix	440-443	4
α-helix	446-447	2
β-strand	474-475	2	1

Chain C: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	8-9	2	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
RAC-alpha serine/threonine-protein kinase	A	protein	341	Homo sapiens	P31749 (AlphaFold model)
Glycogen synthase kinase-3 beta	C	protein	10	Homo sapiens	P49841 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3QKL_1 RAC-alpha serine/threonine-protein kinase (chains A)
GAMARVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTEN
RVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVS
ALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPE
VLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSL
LSGLLKKDPKQRLGGGSEDAKEIMQHRFFAGIVWQHVYEKKLSPPFKPQVTSETDTRYFD
EEFTAQMITITPPDQDDSMECVDSERRPHFPQFDYSASSTA

Sequence of entity 2 (C), FASTA

>3QKL_2 Glycogen synthase kinase-3 beta (chains C)
GRPRTTSFAE

Ligands and cofactors

ID	Name	Formula	Copies
SMR	N-{(2S)-3-[(3S)-8',9'-dihydro-1H,3'H-spiro[piperidine-3,7'-pyrano[3,2-e]indazol…	C29 H40 N4 O5 S	1

Primary citation

Discovery and SAR of spirochromane Akt inhibitors. Kallan, N.C., Spencer, K.L., Blake, J.F. et al. Bioorg Med Chem Lett (2011) 21:2410-2414. DOI 10.1016/j.bmcl.2011.02.073 · 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
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,…
2UZR 1.94 Å, A transforming mutation in the pleckstrin homology domain of AKT1 in cancer (AKT1-PH_E17K)

Browse structure collections

About this viewer

MolViewer shows 3QKL directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.