Research workbench
Crystal structure of mouse TLR4/MD-2/LIPID iva complex
Analyse Crystal structure of mouse TLR4/MD-2/LIPID iva complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3VQ1
- Type
- protein
- Length
- 1,462 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Toll-like receptor 4; Lymphocyte antigen 96
- UniProt
- Q9QUK6, Q9JHF9
- Ligands
- LP4, LP5, NAG
- Pockets
- 9 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 9% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Toll-like receptor 4 | protein | 596 | 10% helix, 22% strand | Q9QUK6 |
| C, D | Lymphocyte antigen 96 | protein | 135 | 3% helix, 55% strand | Q9JHF9 |
Ligands and binding sites
- LP4 · 2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-4-O-phosphono-beta-D-glucopyranose · ligand · 2 copies · chains A, C, B, D
- LP5 · (R)-((2R,3S,4R,5R,6R)-3-hydroxy-2-(hydroxymethyl)-5-((R)-3-hydroxytetradecanamido)-6-(phosphonooxy) tetrahydro-2H-pyran-4-yl) 3-hydroxytetradecanoate · ligand · 2 copies · chains A, C, B, D
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 845 | 0.80 | 0.82 | 59 | LP4, LP5 |
| 2 | 944 | 0.79 | 0.80 | 57 | LP4, LP5 |
| 3 | 1097 | 0.74 | 0.77 | 105 | empty |
| 4 | 641 | 0.72 | 0.79 | 71 | empty |
| 5 | 568 | 0.69 | 0.78 | 58 | empty |
Interfaces
5 interfaces between chains.
- B–D · 1193 Ų buried · 21 hydrogen bonds · protein-protein
- A–C · 1174 Ų buried · 22 hydrogen bonds · protein-protein
- A–B · 676 Ų buried · 7 hydrogen bonds · protein-protein
- A–D · 482 Ų buried · 3 hydrogen bonds · protein-protein
- C–B · 453 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 disulfide, 4 glycan (disulfide, N-glycosylation).
Compared structures
- 3VQ1 · Crystal structure of mouse TLR4/MD-2/lipid IVa 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 Q9JHF9
- Elsewhere: RCSB PDB 3VQ1 · PDBe 3VQ1 · UniProt Q9QUK6 · UniProt Q9JHF9
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