MolNFT v1 · #169699 · protein

Cryo-EM structure of CARD8-card filament

6XKJ · Caspase recruitment domain-containing protein 8: “Cryo-EM structure of CARD8-card filament”. Electron microscopy, 13 pockets (best druggability 0.81). MolNFT v1 #169699 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6XKJ
Type: protein
Length: 1,360 residues
Chains: 16
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Caspase recruitment domain-containing protein 8
UniProt: Q9Y2G2
Pockets: 13 · best druggability 0.81

Structure

electron microscopy · 1 distinct chain · 78% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
C, A, B, D, E, F, G, H, I, J, K, L, M, N, O, P	Caspase recruitment domain-containing protein 8	protein	85	78% helix, 0% strand	Q9Y2G2

Pockets

13 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	1076	0.81	0.82	105	empty
2	1042	0.81	0.82	100	empty
3	523	0.74	0.82	53	empty
4	503	0.74	0.83	60	empty
5	699	0.74	0.80	58	empty

Interfaces

40 interfaces between chains.

G–K · 521 Å² buried · 2 hydrogen bonds · protein-protein
B–F · 518 Å² buried · 3 hydrogen bonds · protein-protein
L–P · 518 Å² buried · 2 hydrogen bonds · protein-protein
F–J · 517 Å² buried · 2 hydrogen bonds · protein-protein
J–N · 516 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

6XKJ · Cryo-EM structure of CARD8-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 Q9Y2G2
Elsewhere: RCSB PDB 6XKJ · PDBe 6XKJ · UniProt Q9Y2G2

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.