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MolNFT v1 · #180936 · protein

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

7LFH · Nacht, lrr and pyd domains-containing protein 3: “Cryo-EM structure of NLRP3 double-ring cage, 6-fold (12-mer)”. Electron microscopy, 20 pockets (best druggability 0.88). MolNFT v1 #180936 on GenesisL1: 3D structure, binding sites…

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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