Crystal structure of the TIR domain of human myeloid differentiation primary response protein 88. Determined by X-ray diffraction at 1.45 Å resolution. Released 10 Apr 2013.
Explore 4EO7 in 3D Show helices and sheets RCSB PDB PDBe
4EO7 contains 15 α-helices and 6 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 156-158 | 3 | |
| β-strand | 161-166 | 6 | 1 |
| α-helix | 169-171 | 3 | |
| α-helix | 172-183 | 12 | |
| β-strand | 191-193 | 3 | 1 |
| α-helix | 196-198 | 3 | |
| β-strand | 205-206 | 2 | 1 |
| α-helix | 209-211 | 3 | |
| α-helix | 212-215 | 4 | |
| β-strand | 216-223 | 8 | 1 |
| α-helix | 227-229 | 3 | |
| α-helix | 231-242 | 12 | |
| α-helix | 244 | 1 | |
| α-helix | 247-251 | 5 | |
| β-strand | 252-256 | 5 | 1 |
| α-helix | 263-265 | 3 | |
| α-helix | 266-268 | 3 | |
| α-helix | 272-273 | 2 | |
| β-strand | 274-275 | 2 | 1 |
| α-helix | 279-281 | 3 | |
| α-helix | 285-294 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Myeloid differentiation primary response protein MyD88 | A | protein | 144 | Homo sapiens | Q99836 (AlphaFold model) |
>4EO7_1 Myeloid differentiation primary response protein MyD88 (chains A) GGVDMPERFDAFICYCPSDIQFVQEMIRQLEQTNYRLKLCVSDRDVLPGTCVWSIASELI EKRCRRMVVVVSDDYLQSKECDFQTKFALSLSPGAHQKRLIPIKYKAMKKEFPSILRFIT VCDYTNPCTKSWFWTRLAKALSLP
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 1 |
Molecular mechanisms for the subversion of MyD88 signaling by TcpC from virulent uropathogenic Escherichia coli. Snyder, G.A., Cirl, C., Jiang, J. et al. Proc Natl Acad Sci U S A (2013) 110:6985-6990. DOI 10.1073/pnas.1215770110 · 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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