The Solution structure of the eTAFH domain of AML1-ETO complexed with HEB peptide. Determined by solution NMR. Released 6 Oct 2009.
Explore 2KNH in 3D Show helices and sheets RCSB PDB PDBe
2KNH contains 6 α-helices and 0 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 | 271-284 | 14 | |
| α-helix | 292-304 | 13 | |
| α-helix | 310-320 | 11 | |
| α-helix | 329-351 | 23 | |
| α-helix | 355-357 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 15-18 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein CBFA2T1 | A | protein | 103 | Homo sapiens | Q06455 (AlphaFold model) |
| Transcription factor 12 | B | protein | 18 | Homo sapiens | Q99081 (AlphaFold model) |
>2KNH_1 Protein CBFA2T1 (chains A) GAMGSGARQLSKLKRFLTTLQQFGNDISPEIGERVRTLVLGLVNSTLTIEEFHSKLQEAT NFPLRPFVIPFLKANLPLLQRELLHCARLAKQNPAQYLAQHEQ
>2KNH_2 Transcription factor 12 (chains B) IGTDKELSDLLDFSAMFS
Structure of the AML1-ETO eTAFH domain-HEB peptide complex and its contribution to AML1-ETO activity. Park, S., Chen, W., Cierpicki, T. et al. Blood (2009) 113:3558-3567. DOI 10.1182/blood-2008-06-161307 · 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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