Research workbench
Cryo-EM structure of pyd-deleted human NLRP3 hexamer
Analyse Cryo-EM structure of pyd-deleted human NLRP3 hexamer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7VTP
- Type
- protein
- Length
- 4,770 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q96P20
- Ligands
- ADP, 7YN
Structure
electron microscopy · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | — | protein | 795 | — | Q96P20 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 6 copies · chains A, B, C, D, E, F
- 7YN · 1-[4-(2-oxidanylpropan-2-yl)furan-2-yl]sulfonyl-3-(1,2, 3,5-tetrahydro-S-indacen-4-yl)urea · ligand · 6 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7VTP · Cryo-EM structure of PYD-deleted human NLRP3 hexamer · the same entry in another collection · chain B against B, TM-score 1.00
- Q96P20 · AlphaFold monomer V2.0 prediction for nacht, lrr and pyd domains- containing protein 3… · a predicted model of the same protein · chain A against A, TM-score 0.69
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 Q96P20
- Elsewhere: RCSB PDB 7VTP · PDBe 7VTP · UniProt Q96P20
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