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Structure of NLRP1 card filament

Analyse Structure of NLRP1 card filament in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6K7V
Type: protein
Length: 1,008 residues
Chains: 12
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nacht, lrr and pyd domains-containing protein 1
UniProt: Q9C000
Pockets: 16 · best druggability 0.85

Structure

electron microscopy · 1 distinct chain · 67% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
J, A, B, C, D, E, F, G, H, I, K, L	Nacht, lrr and pyd domains-containing protein 1	protein	84	67% helix, 0% strand	Q9C000

Pockets

16 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	955	0.85	0.86	155	empty
2	443	0.79	0.87	77	empty
3	444	0.79	0.87	77	empty
4	420	0.77	0.86	61	empty
5	197	0.68	0.86	35	empty

Interfaces

28 interfaces between chains.

C–D · 474 Å² buried · 4 hydrogen bonds · protein-protein
H–I · 462 Å² buried · 3 hydrogen bonds · protein-protein
B–C · 459 Å² buried · 3 hydrogen bonds · protein-protein
A–F · 458 Å² buried · 4 hydrogen bonds · protein-protein
A–L · 457 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

6K7V · Structure of NLRP1 CARD filament · the same entry in another collection · chain L against L, 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 Q9C000
Elsewhere: RCSB PDB 6K7V · PDBe 6K7V · UniProt Q9C000

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