6I3N: Helical MyD88 death domain filament

Helical MyD88 death domain filament. Determined by electron microscopy at 3.1 Å resolution. Released 20 Nov 2019.

Method
Electron microscopy
Resolution
3.1 Å
Organism
Homo sapiens
Chains
13
Atoms
10,660
Mol. weight
229.41 kDa
Released
20 Nov 2019

Explore 6I3N in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6I3N contains 104 α-helices and 0 β-strands across 13 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.

Chains A, B, C, D, E, F, G, H, I, J, K, L and M: 8 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix22-243
α-helix27-3711
α-helix47-537
α-helix58-647
α-helix70-778
α-helix86-9510
α-helix100-1045
α-helix106-12015

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Myeloid differentiation primary response protein MyD88A, B, C, D, E, F, G, H, I, J, K, L, Mprotein162Homo sapiensQ99836 (AlphaFold model)
Sequence of entity 1 (A, B, C, D, E, F, G, H, I, J, K, L, M), FASTA
>6I3N_1 Myeloid differentiation primary response protein MyD88 (chains A, B, C, D, E, F, G, H, I, J, K, L, M)
SNAMAAGGPGAGSAAPVSSTSSLPLAALNMRVRRRLSLFLNVRTQVAADWTALAEEMDFE
YLEIRQLETQADPTGRLLDAWQGRPGASVGRLLELLTKLGRDDVLLELGPSIEEDCQKYI
LKQQQEEAEKPLQVAAVDSSVPRTAELAGITTLDWSHPQFEK

Primary citation

MyD88 Death-Domain Oligomerization Determines Myddosome Architecture: Implications for Toll-like Receptor Signaling. Moncrieffe, M.C., Bollschweiler, D., Li, B. et al. Structure (2020) 28:281-289.e3. DOI 10.1016/j.str.2020.01.003 · PubMed

Other PDB entries of the same protein (UniProt Q99836 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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