Structure of AKT1(E17K) with compound 4. Determined by X-ray diffraction at 1.9 Å resolution. Released 4 Sept 2024.
Explore 8UW9 in 3D Show helices and sheets RCSB PDB PDBe
8UW9 contains 27 α-helices and 27 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 6-15 | 10 | 1 |
| α-helix | 16 | 1 | |
| β-strand | 22-30 | 9 | 1 |
| β-strand | 34 | 1 | 2 |
| β-strand | 35-38 | 4 | 1 |
| α-helix | 50-52 | 3 | |
| 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 | 93-121 | 29 | |
| α-helix | 147-149 | 3 | |
| β-strand | 150-159 | 10 | 3 |
| β-strand | 162-169 | 8 | 3 |
| β-strand | 175-182 | 8 | 3 |
| α-helix | 183-185 | 3 | |
| α-helix | 201-203 | 3 | |
| α-helix | 211-212 | 2 | |
| β-strand | 213-218 | 6 | 3 |
| β-strand | 222-228 | 7 | 3 |
| β-strand | 234 | 1 | 4 |
| α-helix | 235-242 | 8 | |
| α-helix | 247-263 | 17 | |
| α-helix | 264-268 | 5 | |
| α-helix | 277-279 | 3 | |
| β-strand | 280-282 | 3 | 4 |
| β-strand | 288-290 | 3 | 4 |
| α-helix | 313-315 | 3 | |
| α-helix | 318-321 | 4 | |
| α-helix | 329-344 | 16 | |
| α-helix | 354-363 | 10 | |
| α-helix | 364-366 | 3 | |
| 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 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-7 | 5 | 5 |
| β-strand | 11 | 1 | 6 |
| β-strand | 18-25 | 8 | 5 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-39 | 6 | 7 |
| β-strand | 46-51 | 6 | 7 |
| β-strand | 57-59 | 3 | 7 |
| α-helix | 61-63 | 3 | |
| β-strand | 67-72 | 6 | 5 |
| β-strand | 77-82 | 6 | 5 |
| α-helix | 87-89 | 3 | |
| β-strand | 91-97 | 7 | 7 |
| α-helix | 98-102 | 5 | |
| β-strand | 110-112 | 3 | 7 |
| β-strand | 113 | 1 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| RAC-alpha serine/threonine-protein kinase | A | protein | 438 | Homo sapiens | P31749 (AlphaFold model) |
| NB41 | B | protein | 126 | Lama glama |
>8UW9_1 RAC-alpha serine/threonine-protein kinase (chains A) SDVAIVKEGWLHKRGKYIKTWRPRYFLLKNDGTFIGYKERPQDVDQREAPLNNFSVAQCQ LMKTERPRPNTFIIRCLQWTTVIERTFHVETPEEREEWTTAIQTVADGLKKQEEEEMDAS AEHTDMEVSLAKPKHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVA KDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSED RARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKT FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRF PRTLGPEAKSLLSGLLKKDPKQRLGGGSEDAKEIMQHRFFAGIVWQHVYEKKLSPPFKPQ VTSETDTRYFDEEFTAQM
>8UW9_2 NB41 (chains B) QVQLQESGGGLVQAGGSLRLSCAASGIDVRIKTMAWYRQAPGKQRELLASVLVSGSTNYA DPVKGRFTISRDNAKNTVYLQMNKLIPDDTAVYYCNTYGRLRRDVWGPGTQVTVSSHHHH HHEPEA
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 1 |
| XQ2 | N-({4-[(2P)-2-(2-aminopyridin-3-yl)-5-phenyl-3H-imidazo[4,5-b]pyridin-3-yl]phen… | C33 H25 F N6 O3 | 1 |
Water and common crystallization additives (CL, SO4, EDO) are not listed.
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 P31749 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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