4EO7: PDB entry 4EO7

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.

Method
X-ray diffraction
Resolution
1.45 Å
Organism
Homo sapiens
Chains
1
Atoms
1,456
Mol. weight
16.8 kDa
Ligands
MG
Released
10 Apr 2013

Explore 4EO7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 15 helices, 6 β-strands

ElementResiduesLengthSheet
α-helix156-1583
β-strand161-16661
α-helix169-1713
α-helix172-18312
β-strand191-19331
α-helix196-1983
β-strand205-20621
α-helix209-2113
α-helix212-2154
β-strand216-22381
α-helix227-2293
α-helix231-24212
α-helix2441
α-helix247-2515
β-strand252-25651
α-helix263-2653
α-helix266-2683
α-helix272-2732
β-strand274-27521
α-helix279-2813
α-helix285-29410

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Myeloid differentiation primary response protein MyD88Aprotein144Homo sapiensQ99836 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>4EO7_1 Myeloid differentiation primary response protein MyD88 (chains A)
GGVDMPERFDAFICYCPSDIQFVQEMIRQLEQTNYRLKLCVSDRDVLPGTCVWSIASELI
EKRCRRMVVVVSDDYLQSKECDFQTKFALSLSPGAHQKRLIPIKYKAMKKEFPSILRFIT
VCDYTNPCTKSWFWTRLAKALSLP

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg1

Primary citation

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:

Browse structure collections

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