Crystal structure of human Akt2 in complex with GSK690693. Determined by X-ray diffraction at 2.0 Å resolution. Released 21 Oct 2008.
Explore 3D0E in 3D Show helices and sheets RCSB PDB PDBe
3D0E contains 41 α-helices and 28 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 |
|---|---|---|---|
| α-helix | 149-151 | 3 | |
| β-strand | 152-160 | 9 | 1 |
| β-strand | 165-171 | 7 | 1 |
| β-strand | 177-184 | 8 | 1 |
| α-helix | 185-190 | 6 | |
| α-helix | 194-206 | 13 | |
| β-strand | 212 | 1 | 2 |
| α-helix | 213-214 | 2 | |
| β-strand | 215-220 | 6 | 1 |
| β-strand | 224-229 | 6 | 1 |
| β-strand | 236 | 1 | 2 |
| α-helix | 237-244 | 8 | |
| α-helix | 249-268 | 20 | |
| β-strand | 272 | 1 | 3 |
| α-helix | 278-280 | 3 | |
| β-strand | 281-283 | 3 | 2 |
| β-strand | 289-291 | 3 | 2 |
| β-strand | 298 | 1 | 3 |
| β-strand | 307 | 1 | 4 |
| α-helix | 314-316 | 3 | |
| α-helix | 319-322 | 4 | |
| β-strand | 327 | 1 | 4 |
| α-helix | 331-345 | 15 | |
| α-helix | 355-364 | 10 | |
| α-helix | 365-367 | 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 | |
| α-helix | 441-444 | 4 | |
| α-helix | 447-448 | 2 | |
| α-helix | 450-452 | 3 | |
| α-helix | 469-470 | 2 | |
| β-strand | 475-476 | 2 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 149-151 | 3 | |
| β-strand | 152-160 | 9 | 5 |
| β-strand | 165-171 | 7 | 5 |
| β-strand | 177-184 | 8 | 5 |
| α-helix | 185-190 | 6 | |
| α-helix | 194-206 | 13 | |
| β-strand | 212 | 1 | 6 |
| α-helix | 213-214 | 2 | |
| β-strand | 215-220 | 6 | 5 |
| β-strand | 224-229 | 6 | 5 |
| β-strand | 236 | 1 | 6 |
| α-helix | 237-244 | 8 | |
| α-helix | 249-268 | 20 | |
| β-strand | 272 | 1 | 7 |
| α-helix | 278-280 | 3 | |
| β-strand | 281-283 | 3 | 6 |
| β-strand | 289-291 | 3 | 6 |
| β-strand | 298 | 1 | 7 |
| β-strand | 307 | 1 | 8 |
| α-helix | 314-316 | 3 | |
| α-helix | 319-322 | 4 | |
| β-strand | 327 | 1 | 8 |
| α-helix | 331-345 | 15 | |
| α-helix | 355-364 | 10 | |
| α-helix | 365-367 | 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 | |
| α-helix | 441-444 | 4 | |
| α-helix | 447-448 | 2 | |
| α-helix | 450-452 | 3 | |
| β-strand | 475-476 | 2 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| RAC-beta serine/threonine-protein kinase | A, B | protein | 335 | Homo sapiens | P31751 (AlphaFold model) |
>3D0E_1 RAC-beta serine/threonine-protein kinase (chains A, B) KVTMNDFDYLKLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVAHTVTESRVLQ NTRHPFLTALKYAFQTHDRLCFVMEYANGGELFFHLSRERVFTEERARFYGAEIVSALEY LHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGISDGATMKTFCGTPEYLAPEVLEDN DYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFPRTLSPEAKSLLAGLL KKDPKQRLGGGPSDAKEVMEHRFFLSINWQDVVQKKLLPPFKPQVTSEVDTRYFDDEFTA QSITITPPDRYDSLGLLELDQRTHFPQFDYSASIR
| ID | Name | Formula | Copies |
|---|---|---|---|
| G93 | 4-{2-(4-amino-1,2,5-oxadiazol-3-yl)-1-ethyl-7-[(3S)-piperidin-3-ylmethoxy]-1H-i… | C21 H27 N7 O3 | 2 |
Identification of 4-(2-(4-amino-1,2,5-oxadiazol-3-yl)-1-ethyl-7-{[(3S)-3-piperidinylmethyl]oxy}-1H-imidazo[4,5-c]pyridin-4-yl)-2-methyl-3-butyn-2-ol (GSK690693), a novel inhibitor of AKT kinase. Heerding, D.A., Rhodes, N., Leber, J.D. et al. J Med Chem (2008) 51:5663-5679. DOI 10.1021/jm8004527 · PubMed
Other PDB entries of the same protein (UniProt P31751 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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