9C1W: AKT2 with compound 3

Structure of AKT2 with compound 3. Determined by X-ray diffraction at 2.0 Å resolution. Released 4 Sept 2024.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Homo sapiens
Chains: 1
Atoms: 3,389
Mol. weight: 52.66 kDa
Ligands: XOO
Released: 4 Sept 2024

Explore 9C1W in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9C1W contains 21 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: 21 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	6-15	10	1
β-strand	22-30	9	1
β-strand	34	1	2
β-strand	35-38	4	1
α-helix	53-55	3
β-strand	56	1	2
β-strand	61-65	5	1
β-strand	72-79	8	1
β-strand	82-89	8	1
α-helix	93-117	25
α-helix	149-151	3
β-strand	152-160	9	3
β-strand	164-171	8	3
β-strand	177-184	8	3
α-helix	185-187	3
α-helix	197-203	7
α-helix	213-214	2
β-strand	215-220	6	3
β-strand	224-230	7	3
β-strand	236	1	4
α-helix	237-244	8
α-helix	249-268	20
α-helix	278-280	3
β-strand	281-283	3	4
β-strand	289-291	3	4
α-helix	314-316	3
α-helix	319-322	4
α-helix	330-345	16
α-helix	355-364	10
α-helix	365-367	3
α-helix	375-384	10
α-helix	389-391	3
α-helix	400-404	5
α-helix	407-409	3
α-helix	414-418	5
α-helix	423-424	2
α-helix	437-439	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
RAC-beta serine/threonine-protein kinase	A	protein	446	Homo sapiens	P31751 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>9C1W_1 RAC-beta serine/threonine-protein kinase (chains A)
NEVSVIKEGWLHKRGEYIKTWRPRYFLLKSDGSFIGYKERPEAPDQTLPPLNNFSVAECQ
LMKTERPRPNTFVIRCLQWTTVIERTFHVDSPDEREEWMRAIQMVANSLKQRAAAEDPMD
YKCGSPSDSSTTEEMEVAVSKARAKVTMNDFDYLKLLGKGTFGKVILVREKATGRYYAMK
ILRKEVIIAKDEVAHTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGELFFHL
SRERVFTEERARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGI
SDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFEL
ILMEEIRFPRTLSPEAKSLLAGLLKKDPKQRLGGGPSDAKEVMEHRFFLSINWQDVVQKK
LLPPFKPQVTSEVDTRYFDDEFTAQS

Ligands and cofactors

ID	Name	Formula	Copies
XOO	4-{2-[({4-[(2P)-2-(2-aminopyridin-3-yl)-5-phenyl-3H-imidazo[4,5-b]pyridin-3-yl]…	C33 H28 N6 O2	1

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

Primary citation

Mutant-selective AKT inhibition through lysine targeting and neo-zinc chelation. Craven, G.B., Chu, H., Sun, J.D. et al. Nature (2025) 637:205-214. DOI 10.1038/s41586-024-08176-4 · PubMed

Other PDB entries of the same protein (UniProt P31751 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1O6L 1.6 Å, Crystal structure of an activated Akt/protein kinase B (PKB-PIF chimera) ternary complex…
1O6K 1.7 Å, Structure of activated form of PKB kinase domain S474D with GSK3 peptide and AMP-PNP
2JDO 1.8 Å, Structure of pkb-beta (AKT2) complexed with isoquinoline-5-sulfonic acid…
2X39 1.93 Å, Structure of 4-Amino-N-(4-chlorobenzyl)-1-(7H-pyrrolo(2,3-d)pyrimidin-…
3D0E 2.0 Å, Crystal structure of human Akt2 in complex with GSK690693
2UW9 2.1 Å, STRUCTURE OF PKB-BETA (AKT2) COMPLEXED WITH 4-(4-chloro-phenyl)-4-(4-(1H-pyrazol-4-yl)-ph…
1GZK 2.3 Å, Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif…
2JDR 2.3 Å, Structure of pkb-beta (AKT2) complexed with the inhibitor a-443654
3E87 2.3 Å, Crystal structures of the kinase domain of AKT2 in complex with ATP-competitive inhibitors
8Q61 2.32 Å, Co-crystal structure of human AKT2 with compound 3
1GZN 2.5 Å, Structure of PKB kinase domain
3E88 2.5 Å, Crystal structures of the kinase domain of AKT2 in complex with ATP-competitive inhibitors

Browse structure collections

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