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Lrr domain from human NLRP1

Analyse Lrr domain from human NLRP1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4IM6
Type
protein
Length
198 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Nacht, lrr and pyd domains-containing protein 1
UniProt
Q9C000
Pockets
1 · best druggability 0.57

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 12% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ANacht, lrr and pyd domains-containing protein 1protein19843% helix, 12% strandQ9C000

Ligands and binding sites

  • GOL · Glycerol · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1730.570.8814empty

Modifications

Observed in the structure: 1 modified (oxidation).

Compared structures

  • 4IM6 · LRR domain from human NLRP1 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9C000 · AlphaFold monomer V2.0 prediction for nacht, lrr and pyd domains- containing protein 1… · a predicted model of the same protein · chain A against A, TM-score 0.97

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