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Cryo-EM structure of NLRP3 double-ring cage, 6-fold (12-mer)

Analyse Cryo-EM structure of NLRP3 double-ring cage, 6-fold (12-mer) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7LFH
Type
protein
Length
9,672 residues
Chains
12
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Nacht, lrr and pyd domains-containing protein 3
UniProt
Q8R4B8
Pockets
20 · best druggability 0.88

Structure

electron microscopy · 1 distinct chain · 41% helix, 10% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, LNacht, lrr and pyd domains-containing protein 3protein80641% helix, 10% strandQ8R4B8

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18250.880.90106empty
27550.880.91103empty
36970.870.91108empty
49490.870.88117empty
510120.870.88124empty

Interfaces

24 interfaces between chains.

  • H–I · 1587 Ų buried · 4 hydrogen bonds · protein-protein
  • D–E · 1572 Ų buried · 4 hydrogen bonds · protein-protein
  • A–L · 1558 Ų buried · 4 hydrogen bonds · protein-protein
  • F–G · 1551 Ų buried · 4 hydrogen bonds · protein-protein
  • B–C · 1538 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

  • 7LFH · Cryo-EM structure of NLRP3 double-ring cage, 6-fold (12-mer) · the same entry in another collection · chain L against L, TM-score 1.00

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