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Cryo-EM structure of NLRC4-card filament

Analyse Cryo-EM structure of NLRC4-card filament in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6N1I
Type: protein
Length: 1,360 residues
Chains: 16
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nlr family card domain-containing protein 4
UniProt: Q9NPP4
Pockets: 20 · best druggability 0.84

Structure

electron microscopy · 1 distinct chain · 71% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P	Nlr family card domain-containing protein 4	protein	85	71% helix, 0% strand	Q9NPP4

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	884	0.84	0.86	85	empty
2	464	0.78	0.86	43	empty
3	381	0.78	0.88	42	empty
4	458	0.78	0.86	45	empty
5	421	0.77	0.86	45	empty

Interfaces

40 interfaces between chains.

A–N · 554 Å² buried · 5 hydrogen bonds · protein-protein
A–D · 552 Å² buried · 5 hydrogen bonds · protein-protein
I–L · 550 Å² buried · 5 hydrogen bonds · protein-protein
C–P · 549 Å² buried · 5 hydrogen bonds · protein-protein
B–O · 548 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

6N1I · Cryo-EM structure of NLRC4-CARD filament · the same entry in another collection · chain P against P, TM-score 1.00

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 Q9NPP4
Elsewhere: RCSB PDB 6N1I · PDBe 6N1I · UniProt Q9NPP4

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