Research workbench

Helical assembly of the CARD9 card

Analyse Helical assembly of the CARD9 card in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6N2P
Type: protein
Length: 880 residues
Chains: 10
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Caspase recruitment domain-containing protein 9
UniProt: Q9H257
Pockets: 12 · best druggability 0.81

Structure

electron microscopy · 1 distinct chain · 69% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J	Caspase recruitment domain-containing protein 9	protein	88	69% helix, 0% strand	Q9H257

Pockets

12 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	419	0.81	0.89	74	empty
2	203	0.72	0.89	34	empty
3	174	0.70	0.89	37	empty
4	183	0.70	0.88	27	empty
5	121	0.65	0.88	27	empty

Interfaces

30 interfaces between chains.

B–E · 454 Å² buried · 5 hydrogen bonds · protein-protein
C–F · 450 Å² buried · 5 hydrogen bonds · protein-protein
B–H · 448 Å² buried · 5 hydrogen bonds · protein-protein
A–I · 444 Å² buried · 5 hydrogen bonds · protein-protein
A–D · 441 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

6N2P · Helical assembly of the CARD9 CARD · the same entry in another collection · chain J against J, TM-score 1.00
Q9H257 · AlphaFold monomer V2.0 prediction for caspase recruitment domain- containing protein 9… · a predicted model of the same protein · chain J against A, TM-score 0.91

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 Q9H257
Elsewhere: RCSB PDB 6N2P · PDBe 6N2P · UniProt Q9H257

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