2Z5V: TIR domain of human MyD88

Solution structure of the TIR domain of human MyD88. Determined by solution NMR. Released 5 Aug 2008.

Method
Solution NMR
Organism
Homo sapiens
Chains
1
Atoms
1,159
Mol. weight
17.39 kDa
Released
5 Aug 2008

Explore 2Z5V in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2Z5V contains 5 α-helices and 5 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: 5 helices, 5 β-strands

ElementResiduesLengthSheet
β-strand16-1941
α-helix25-3612
β-strand44-4521
β-strand71-7551
α-helix78-814
α-helix84-9411
β-strand105-10951
β-strand127-12821
α-helix132-1354
α-helix138-1469

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Myeloid differentiation primary response protein MyD88Aprotein149Homo sapiensQ99836 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2Z5V_1 Myeloid differentiation primary response protein MyD88 (chains A)
TTLDDPLGHMPERFDAFICYCPSDIQFVQEMIRQLEQTNYRLKLCVSDRDVLPGTCVWSI
ASELIEKRCRRMVVVVSDDYLQSKECDFQTKFALSLSPGAHQKRLIPIKYKAMKKEFPSI
LRFITVCDYTNPCTKSWFWTRLAKALSLP

Primary citation

Structural basis for the multiple interactions of the MyD88 TIR domain in TLR4 signaling. Ohnishi, H., Tochio, H., Kato, Z. et al. Proc Natl Acad Sci U S A (2009). DOI 10.1073/pnas.0812956106 · 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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