Research workbench
Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide
Analyse Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Z82
- Type
- protein
- Length
- 550 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9QUN7, Q4G1L2
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 550 | — | Q9QUN7, Q4G1L2 |
Compared structures
- 2Z82 · Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9QUN7 · AlphaFold monomer V2.0 prediction for toll-like receptor 2 (Q9QUN7) · a predicted model of the same protein · chain A against A, TM-score 0.98
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q9QUN7
- Every structure of UniProt Q4G1L2
- Elsewhere: RCSB PDB 2Z82 · PDBe 2Z82 · UniProt Q9QUN7 · UniProt Q4G1L2
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