2L11: Cbx3

Solution NMR structure of the Cbx3 in complex with H3K9me3 peptide. Determined by solution NMR. Released 4 Aug 2010.

Method
Solution NMR
Organisms
Homo sapiens, Xenopus laevis
Chains
2
Atoms
561
Mol. weight
7.96 kDa
Released
4 Aug 2010

Explore 2L11 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 1 helix, 4 β-strands

ElementResiduesLengthSheet
β-strand2-14131
β-strand17-2481
β-strand34-3631
β-strand4011
α-helix43-5311
Chain B: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand5-841

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Chromobox protein homolog 3Aprotein54Homo sapiensQ13185 (AlphaFold model)
Histone H3Bprotein15Xenopus laevisP84233 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2L11_1 Chromobox protein homolog 3 (chains A)
GEFVVEKVLDRRVVNGKVEYFLKWKGFTDADNTWEPEENLDCPELIEAFLNSQK
Sequence of entity 2 (B), FASTA
>2L11_2 Histone H3 (chains B)
ARTKQTARKSTGGKA

Primary citation

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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