8Q61: RAC-beta serine/threonine-protein kinase

Co-crystal structure of human AKT2 with compound 3. Determined by X-ray diffraction at 2.32 Å resolution. Released 16 Aug 2023.

Method: X-ray diffraction
Resolution: 2.32 Å
Organism: Homo sapiens
Chains: 1
Atoms: 3,371
Mol. weight: 56.99 kDa
Ligands: K06, PO4
Released: 16 Aug 2023

Explore 8Q61 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8Q61 contains 16 α-helices and 18 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: 16 helices, 18 β-strands

Element	Residues	Length	Sheet
α-helix	3-4	2
β-strand	6-15	10	1
β-strand	19	1	2
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	93-109	17
α-helix	149-151	3
β-strand	152-161	10	3
β-strand	164-171	8	3
β-strand	177-183	7	3
α-helix	191-203	13
β-strand	212	1	4
β-strand	215-220	6	3
β-strand	225-229	5	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
β-strand	301	1	2
α-helix	319-322	4
α-helix	330-345	16
α-helix	358-364	7
α-helix	366-368	3
α-helix	375-384	10
α-helix	400-404	5
α-helix	407-409	3
α-helix	414-418	5
α-helix	423-424	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
RAC-beta serine/threonine-protein kinase	A	protein	483	Homo sapiens	P31751 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>8Q61_1 RAC-beta serine/threonine-protein kinase (chains A)
GAMDEVSVIKEGWLHKRGEYIKTWRPRYFLLKSDGSFIGYKERPEAPDQTLPPLNNFSVA
ECQLMKTERPRPNTFVIRCLQWTTVIERTFHVDSPDEREEWMRAIQMVANSLKQRAPGED
PMDYKCGSPSDSSTTEEMEVAVSKARAKVTMNDFDYLKLLGKGTFGKVILVREKATGRYY
AMKILRKEVIIAKDEVAHTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGELF
FHLSRERVFTEERARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCK
EGISDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERL
FELILMEEIRFPRTLSPEAKSLLAGLLKKDPKQRLGGGPSDAKEVMEHRFFLSINWQDVV
QKKLLPPFKPQVTSEVDTRYFDDEFTAQSITITPPDRYDSLGLLELDQRTHFPQFSYSAS
IRE

Ligands and cofactors

ID	Name	Formula	Copies
K06	6-[4-(1-azanyl-3-methyl-3-oxidanyl-cyclobutyl)phenyl]-7-phenyl-1-propyl-pyrido[…	C27 H29 N3 O3	1
PO4	Phosphate ion	O4 P	3

Water and common crystallization additives (GOL, MES) are not listed.

Primary citation

Identification and development of a subtype-selective allosteric AKT inhibitor suitable for clinical development. Page, N., Wappett, M., O'Dowd, C.R. et al. Sci Rep (2022) 12:15715. DOI 10.1172/JCI41680 · 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
9C1W 2.0 Å, Structure of AKT2 with compound 3
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
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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