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AlphaFold monomer V2.0 prediction for nacht, lrr and pyd domains- containing protein 3 (Q8R4B8)

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: Q8R4B8
Type: protein
Length: 1,033 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0xb3c0C983Fc44934AC589D7131C08a72544EBB92E
Molecule: Nacht, lrr and pyd domains-containing protein 3
UniProt: Q8R4B8
Pockets: 12 · best druggability 0.83

Structure

1 distinct chain · 46% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nacht, lrr and pyd domains-containing protein 3	protein	1033	46% helix, 11% strand	Q8R4B8

Pockets

12 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1012	0.83	0.84	93	empty
2	597	0.75	0.82	57	empty
3	109	0.50	0.81	16	empty
4	188	0.50	0.77	25	empty
5	129	0.41	0.75	18	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

7VTQ · Cryo-EM structure of mouse NLRP3 (full-length) dodecamer · an experimental structure of the same protein · chain A against I, TM-score 0.58
7VTQ · Cryo-EM structure of mouse NLRP3 (full-length) dodecamer · an experimental structure of the same protein · chain A against A, TM-score 0.58

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 Q8R4B8
Elsewhere: UniProt Q8R4B8 · AlphaFold DB Q8R4B8

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