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AlphaFold monomer V2.0 prediction for nacht, lrr and pyd domains- containing protein 3 (Q96P20)

Analyse AlphaFold monomer V2.0 prediction for nacht, lrr and pyd domains- containing… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: Q96P20
Type: protein
Length: 1,036 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x07769FccfCA38eD8b3F70D165ddF64fA6c8EB6b2
Molecule: Nacht, lrr and pyd domains-containing protein 3
UniProt: Q96P20
Pockets: 12 · best druggability 0.75

Structure

1 distinct chain · 47% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nacht, lrr and pyd domains-containing protein 3	protein	1036	47% helix, 11% strand	Q96P20

Pockets

12 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	845	0.75	0.79	64	empty
2	544	0.73	0.81	85	empty
3	56	0.62	0.92	15	empty
4	367	0.60	0.77	38	empty
5	155	0.52	0.80	23	empty

Compared structures

8EJ4 · Cryo-EM structure of the active NLRP3 inflammasome disk · an experimental structure of the same protein · chain A against D, TM-score 0.74
8SWF · Cryo-EM structure of NLRP3 open octamer · an experimental structure of the same protein · chain A against D, TM-score 0.60

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: UniProt Q96P20 · AlphaFold DB Q96P20

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