3MOP: PDB entry 3MOP
The ternary Death Domain complex of MyD88, IRAK4, and IRAK2. Determined by X-ray diffraction at 3.4 Å resolution. Released 2 Jun 2010.
- Method
- X-ray diffraction
- Resolution
- 3.4 Å
- Organism
- Homo sapiens
- Chains
- 14
- Atoms
- 11,534
- Mol. weight
- 179.46 kDa
- Released
- 2 Jun 2010
Explore 3MOP in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
3MOP contains 111 α-helices and 24 β-strands across 14 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 and B: 8 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 22-24 | 3 | |
| α-helix | 27-37 | 11 | |
| α-helix | 47-51 | 5 | |
| α-helix | 58-64 | 7 | |
| α-helix | 70-79 | 10 | |
| α-helix | 86-96 | 11 | |
| α-helix | 99-102 | 4 | |
| α-helix | 106-112 | 7 | |
Chains C and F: 9 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 22-24 | 3 | |
| α-helix | 28-37 | 10 | |
| α-helix | 47-53 | 7 | |
| α-helix | 58-62 | 5 | |
| α-helix | 70-75 | 6 | |
| α-helix | 87-95 | 9 | |
| α-helix | 101-104 | 4 | |
| α-helix | 106-112 | 7 | |
| α-helix | 114-117 | 4 | |
Chains D and E: 7 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 22-24 | 3 | |
| α-helix | 28-37 | 10 | |
| α-helix | 47-53 | 7 | |
| α-helix | 58-62 | 5 | |
| α-helix | 70-79 | 10 | |
| α-helix | 86-95 | 10 | |
| α-helix | 99-113 | 15 | |
Chains G, H and J: 8 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 10 | 1 | 1 |
| α-helix | 11-13 | 3 | |
| α-helix | 16-26 | 11 | |
| α-helix | 31-38 | 8 | |
| β-strand | 40 | 1 | 2 |
| β-strand | 46 | 1 | 2 |
| α-helix | 50-57 | 8 | |
| α-helix | 58-60 | 3 | |
| α-helix | 66-73 | 8 | |
| β-strand | 80 | 1 | 1 |
| α-helix | 81-89 | 9 | |
| α-helix | 94-100 | 7 | |
Chain I: 7 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 10 | 1 | 5 |
| α-helix | 11-13 | 3 | |
| α-helix | 16-26 | 11 | |
| α-helix | 31-38 | 8 | |
| β-strand | 40 | 1 | 6 |
| β-strand | 46 | 1 | 6 |
| α-helix | 50-57 | 8 | |
| α-helix | 66-73 | 8 | |
| β-strand | 80 | 1 | 5 |
| α-helix | 81-89 | 9 | |
| α-helix | 94-100 | 7 | |
Chains K, L, M and N: 8 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4 | 1 | 9 |
| α-helix | 5-7 | 3 | |
| α-helix | 10-16 | 7 | |
| α-helix | 25-32 | 8 | |
| α-helix | 39-47 | 9 | |
| α-helix | 48-50 | 3 | |
| α-helix | 56-65 | 10 | |
| β-strand | 70 | 1 | 9 |
| α-helix | 72-76 | 5 | |
| α-helix | 84-87 | 4 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Myeloid differentiation primary response protein MyD88 | A, B, C, D, E, F | protein | 110 | Homo sapiens | Q99836 (AlphaFold model) |
| Interleukin-1 receptor-associated kinase 4 | G, H, I, J | protein | 113 | Homo sapiens | Q9NWZ3 (AlphaFold model) |
| Interleukin-1 receptor-associated kinase-like 2 | K, L, M, N | protein | 111 | Homo sapiens | O43187 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E, F), FASTA
>3MOP_1 Myeloid differentiation primary response protein MyD88 (chains A, B, C, D, E, F)
MLPLAALNMRVRRRLSLFLNVRTQVAADWTALAEEMDFEYLEIRQLETQADPTGRLLDAW
QGRPGASVGRLLELLTKLGRDDVLLELGPSIEEDCQKYIAAALEHHHHHH
Sequence of entity 2 (G, H, I, J), FASTA
>3MOP_2 Interleukin-1 receptor-associated kinase 4 (chains G, H, I, J)
MGPITPSTYVRCLNVGLIRKLSDFIDPQEGWKKLAVAIKKPSGDDRYNQFHIRRFEALLQ
TGKSPTSELLFDWGTTNCTVGDLVDLLIQNEFFAPASLLLPDAVPLEHHHHHH
Sequence of entity 3 (K, L, M, N), FASTA
>3MOP_3 Interleukin-1 receptor-associated kinase-like 2 (chains K, L, M, N)
ACYIYQLPSWVLDDLCRNMDALSEWDWMEFASYVITDLTQLRKIKSMEWVQGVSITRELL
WWWGMRQATVQQLVDLLCRLELYRAAQIILNWKPAPEIRCPIPAFPDSVKP
Primary citation
Helical assembly in the MyD88-IRAK4-IRAK2 complex in TLR/IL-1R signalling. Lin, S.C., Lo, Y.C., Wu, H. Nature (2010) 465:885-890. DOI 10.1038/nature09121 · PubMed
Other PDB entries of the same protein (UniProt Q99836 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 4EO7 1.45 Å, Crystal structure of the TIR domain of human myeloid differentiation primary response…
- 9HFV 1.45 Å, MyD88 peptide_2 bound to SPOP MATH domain
- 4DOM 1.8 Å, Crystal Structure of the TIR-domain of Human Myeloid Differentiation Primary Response…
- 9HGH 1.9 Å, MyD88 peptide_1 bound to SPOP MATH domain
- 7BER 2.3 Å, SFX structure of the MyD88 TIR domain higher-order assembly (solved, rebuilt and refined…
- 7L6W 2.3 Å, SFX structure of the MyD88 TIR domain higher-order assembly
- 8S78 2.85 Å, MicroED Structure of TLR2 TIR domain-induced MyD88 TIR domain higher-order assembly
- 7BEQ 3.0 Å, MicroED structure of the MyD88 TIR domain higher-order assembly
- 6I3N 3.1 Å, Helical MyD88 death domain filament
- 8W8M 3.28 Å, Cryo-EM structure of helical filament of MyD88 TIR
- 8YYM 3.3 Å, Cryo-EM structure of cylindrical fiber of MyD88 TIR
- 2JS7 Solution NMR structure of human myeloid differentiation primary response (MyD88).…
Browse structure collections
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