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3D NMR solution structure of NLRP3 pyd

Analyse 3D NMR solution structure of NLRP3 pyd in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2NAQ
Type: protein
Length: 91 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nacht, lrr and pyd domains-containing protein 3
UniProt: Q96P20
Pockets: 2 · best druggability 0.70

Structure

solution nmr · 1 distinct chain · 73% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nacht, lrr and pyd domains-containing protein 3	protein	91	73% helix, 0% strand	Q96P20

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	152	0.70	0.89	26	empty
2	80	0.54	0.85	18	empty

Compared structures

2NAQ · 3D NMR solution structure of NLRP3 PYD · the same entry in another collection · chain A against A, 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 0.73

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 2NAQ · PDBe 2NAQ · UniProt Q96P20

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