2KYG: PDB entry 2KYG

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.

Method
Solution NMR
Organism
Homo sapiens
Chains
3
Atoms
1,082
Mol. weight
15.43 kDa
Released
20 Oct 2010

Explore 2KYG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 2 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix9-2315
α-helix28-4114
Chain B: 2 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix9-2315
α-helix28-4215
Chain C: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix592-61322

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
cAMP-dependent protein kinase type II-alpha regulatory subunitA, Bprotein50Homo sapiensP13861 (AlphaFold model)
Protein CBFA2T1Cprotein38Homo sapiensQ06455 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>2KYG_1 cAMP-dependent protein kinase type II-alpha regulatory subunit (chains A, B)
GAMGSMSHIQIPPGLTELLQGYTVEVLRQQPPDLVEFAVEYFTRLREARA
Sequence of entity 2 (C), FASTA
>2KYG_2 Protein CBFA2T1 (chains C)
AMADIGSASGYVPEEIWKKAEEAVNEVKRQAMTELQKA

Primary citation

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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