Research workbench
Cryo-EM structure of mouse NLRP3 (full-length) dodecamer
Analyse Cryo-EM structure of mouse NLRP3 (full-length) dodecamer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7VTQ
- Type
- protein
- Length
- 9,468 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q8R4B8
- Ligands
- ADP, 7YN
Structure
electron microscopy · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L | — | protein | 789 | — | Q8R4B8 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 12 copies · chains A, B, C, D, E, F, G, H, I, J, K, L
- 7YN · 1-[4-(2-oxidanylpropan-2-yl)furan-2-yl]sulfonyl-3-(1,2, 3,5-tetrahydro-S-indacen-4-yl)urea · ligand · 12 copies · chains A, B, C, D, E, F, G, H, I, J, K, L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7VTQ · Cryo-EM structure of mouse NLRP3 (full-length) dodecamer · the same entry in another collection · chain L against L, TM-score 1.00
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 Q8R4B8
- Elsewhere: RCSB PDB 7VTQ · PDBe 7VTQ · UniProt Q8R4B8
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