Research workbench

AlphaFold monomer V2.0 prediction for protein NLRC5 (C3VPR6)

Analyse AlphaFold monomer V2.0 prediction for protein NLRC5 (C3VPR6) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: C3VPR6
Type: protein
Length: 1,915 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x7a1388B6Aad67B04634A32f63b8A6D6005eab86c
Molecule: Protein NLRC5
UniProt: C3VPR6
Pockets: 18 · best druggability 0.84

Structure

1 distinct chain · 40% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein NLRC5	protein	1915	40% helix, 16% strand	C3VPR6

Pockets

18 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	988	0.84	0.85	70	empty
2	575	0.80	0.86	71	empty
3	427	0.72	0.83	49	empty
4	475	0.72	0.81	48	empty
5	378	0.69	0.82	47	empty

Compared structures

2MJM · The solution NMR structure of the NLRC5 caspase recruitment domain (CARD) · an experimental structure of the same protein · chain A against A, TM-score 0.04
2MJM · The solution NMR structure of the NLRC5 caspase recruitment domain (card) · an experimental structure of the same protein · chain A against A, TM-score 0.04

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 C3VPR6
Elsewhere: UniProt C3VPR6 · AlphaFold DB C3VPR6

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