Research workbench
The crystal structure of mouse TLR4/MD-2/NEOSEPTIN-3 complex
Analyse The crystal structure of mouse TLR4/MD-2/NEOSEPTIN-3 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5IJC
- Type
- protein
- Length
- 1,454 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9QUK6, Q4G1L2, Q9JHF9
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 589 | — | Q9QUK6, Q4G1L2 |
| C, D | — | protein | 136 | — | Q9JHF9 |
| B | — | protein | 593 | — | Q9QUK6, Q4G1L2 |
Compared structures
- 5IJC · The crystal structure of mouse TLR4/MD-2/neoseptin-3 complex · the same entry in another collection · chain A against A, TM-score 1.00
- Q9QUK6 · AlphaFold monomer V2.0 prediction for toll-like receptor 4 (Q9QUK6) · a predicted model of the same protein · chain A against A, TM-score 0.99
- Q9JHF9 · AlphaFold monomer V2.0 prediction for lymphocyte antigen 96 (Q9JHF9) · a predicted model of the same protein · chain C against A, TM-score 0.94
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 Q9QUK6
- Every structure of UniProt Q4G1L2
- Every structure of UniProt Q9JHF9
- Elsewhere: RCSB PDB 5IJC · PDBe 5IJC · UniProt Q9QUK6 · UniProt Q4G1L2 · UniProt Q9JHF9
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