9TMV: Akt1 mutant

Akt1 mutant in complex with the 3-ethyl 1-methyl 1,4-substituted pyrazole containing compound and EG. Determined by X-ray diffraction at 1.9 Å resolution. Released 16 Sept 2026.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: Homo sapiens
Chains: 1
Atoms: 3,306
Mol. weight: 52.39 kDa
Ligands: A1JWX
Released: 16 Sept 2026

Explore 9TMV in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9TMV contains 18 α-helices and 16 β-strands across 1 chain. 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: 18 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	6-15	10	1
β-strand	22-30	9	1
β-strand	34-38	5	1
β-strand	53-56	4	1
β-strand	61-65	5	1
β-strand	72-79	8	1
β-strand	82-89	8	1
α-helix	93-111	19
α-helix	147-149	3
β-strand	150-158	9	2
β-strand	162-169	8	2
β-strand	175-182	8	2
α-helix	183-185	3
α-helix	196-198	3
α-helix	200-202	3
β-strand	210	1	3
β-strand	213-218	6	2
β-strand	222-228	7	2
β-strand	234	1	3
α-helix	235-242	8
α-helix	247-266	20
α-helix	277-279	3
β-strand	280-282	3	3
β-strand	288-290	3	3
α-helix	313-315	3
α-helix	318-321	4
α-helix	329-344	16
α-helix	354-363	10
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	422-423	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
RAC-alpha serine/threonine-protein kinase	A	protein	445	Homo sapiens	P31749 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>9TMV_1 RAC-alpha serine/threonine-protein kinase (chains A)
GSDVAIVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPQDVDQREAPLNNFSVAQC
QLMKTERPRPNTFIIRCLQWTTVIERTFHVETPEEREEWTTAIQTVADGLKKQAAAEMDF
RSGSPSDNSGAEEMEVSLAKPKHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKI
LKKEVIVAKDEVAHTLTENRVLQNTRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLS
RERVFSEDRARFYGAEIVSALEYLHSRDVVYRDLKLENLMLDKDGHIKITDFGLCKEGIK
DGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELI
LMEEIRFPRTLGPEAKSLLSGLLKKDPKQRLGGGSEDAKEIMQHRFFAGIVWQHVYEKKL
SPPFKPQVTSETDTRYFDEEFTAQM

Ligands and cofactors

ID	Name	Formula	Copies
A1JWX	~{N}-[3-[1-[[4-[5-[(3-ethyl-1-methyl-pyrazol-4-yl)methyl]-3-phenyl-pyridin-2-yl…	C40 H43 N7 O2	1

Water and common crystallization additives (EDO) are not listed.

Primary citation

Isoform-Selective Targeting of Akt Through Covalent Allosteric Inhibition. D'Angelo, G.D., Pervanidis, K.A., Athanasiadis, I. et al. Angew Chem Int Ed Engl (2026):e3567206-e3567206. DOI 10.1002/anie.3567206 · 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
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

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