2OD1: MYND domain from human AML1-ETO

Solution structure of the MYND domain from human AML1-ETO. Determined by solution NMR. Released 19 Jun 2007.

Method
Solution NMR
Organism
Homo sapiens
Chains
1
Atoms
392
Mol. weight
6.67 kDa
Ligands
ZN
Released
19 Jun 2007

Explore 2OD1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2OD1 contains 1 α-helix and 2 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: 1 helix, 2 β-strands

ElementResiduesLengthSheet
β-strand672-67321
β-strand681-68221
α-helix685-69511

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Protein CBFA2T1Aprotein60Homo sapiensQ06455 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2OD1_1 Protein CBFA2T1 (chains A)
GSPNSGSPNSDSSESCWNCGRKASETCSGCNTARYCGSFCQHKDWEKHHHICGQTLQAQQ

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn2

Primary citation

Structural basis for recognition of SMRT/N-CoR by the MYND domain and its contribution to AML1/ETO's activity. Liu, Y., Chen, W., Gaudet, J. et al. Cancer Cell (2007) 11:483-497. DOI 10.1016/j.ccr.2007.04.010 · PubMed

Other PDB entries of the same protein (UniProt Q06455 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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