Solution NMR structure of the Cbx3 in complex with H3K9me3 peptide. Determined by solution NMR. Released 4 Aug 2010.
Explore 2L11 in 3D Show helices and sheets RCSB PDB PDBe
2L11 contains 1 α-helix and 5 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 |
|---|---|---|---|
| β-strand | 2-14 | 13 | 1 |
| β-strand | 17-24 | 8 | 1 |
| β-strand | 34-36 | 3 | 1 |
| β-strand | 40 | 1 | 1 |
| α-helix | 43-53 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-8 | 4 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Chromobox protein homolog 3 | A | protein | 54 | Homo sapiens | Q13185 (AlphaFold model) |
| Histone H3 | B | protein | 15 | Xenopus laevis | P84233 (AlphaFold model) |
>2L11_1 Chromobox protein homolog 3 (chains A) GEFVVEKVLDRRVVNGKVEYFLKWKGFTDADNTWEPEENLDCPELIEAFLNSQK
>2L11_2 Histone H3 (chains B) ARTKQTARKSTGGKA
Recognition and specificity determinants of the human cbx chromodomains. Kaustov, L., Ouyang, H., Amaya, M. et al. J Biol Chem (2011) 286:521-529. DOI 10.1074/jbc.M110.191411 · PubMed
Other PDB entries of the same protein (UniProt Q13185 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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