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Cryo-EM structure of asc-card filament

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

PDB: 6N1H
Type: protein
Length: 1,328 residues
Chains: 16
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Apoptosis-associated speck-like protein containing a card
UniProt: Q9ULZ3
Pockets: 20 · best druggability 0.81

Structure

electron microscopy · 1 distinct chain · 69% helix, 2% 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	Apoptosis-associated speck-like protein containing a card	protein	83	69% helix, 2% strand	Q9ULZ3

Pockets

20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	820	0.81	0.84	84	empty
2	522	0.77	0.85	53	empty
3	270	0.70	0.85	29	empty
4	262	0.69	0.85	32	empty
5	268	0.69	0.84	31	empty

Interfaces

40 interfaces between chains.

B–F · 528 Å² buried · 13 hydrogen bonds · protein-protein
I–M · 492 Å² buried · 6 hydrogen bonds · protein-protein
E–I · 492 Å² buried · 6 hydrogen bonds · protein-protein
H–L · 489 Å² buried · 6 hydrogen bonds · protein-protein
L–P · 489 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

6N1H · Cryo-EM structure of ASC-CARD filament · the same entry in another collection · chain K against K, 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 Q9ULZ3
Elsewhere: RCSB PDB 6N1H · PDBe 6N1H · UniProt Q9ULZ3

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