Structure of the AML1-ETO Nervy Domain - PKA(RIIa) complex and its contribution to AML1-ETO activity. Determined by solution NMR. Released 20 Oct 2010.
Explore 2KYG in 3D Show helices and sheets RCSB PDB PDBe
2KYG contains 5 α-helices and 0 β-strands across 3 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 | 9-23 | 15 | |
| α-helix | 28-41 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 9-23 | 15 | |
| α-helix | 28-42 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 592-613 | 22 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| cAMP-dependent protein kinase type II-alpha regulatory subunit | A, B | protein | 50 | Homo sapiens | P13861 (AlphaFold model) |
| Protein CBFA2T1 | C | protein | 38 | Homo sapiens | Q06455 (AlphaFold model) |
>2KYG_1 cAMP-dependent protein kinase type II-alpha regulatory subunit (chains A, B) GAMGSMSHIQIPPGLTELLQGYTVEVLRQQPPDLVEFAVEYFTRLREARA
>2KYG_2 Protein CBFA2T1 (chains C) AMADIGSASGYVPEEIWKKAEEAVNEVKRQAMTELQKA
Structure of the AML1-ETO NHR3-PKA(RIIalpha) complex and its contribution to AML1-ETO activity. Corpora, T., Roudaia, L., Oo, Z.M. et al. J Mol Biol (2010) 402:560-577. DOI 10.1016/j.jmb.2010.08.007 · PubMed
Other PDB entries of the same protein (UniProt P13861 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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