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Cryo-EM structure of AIM2-pyd filament

Analyse Cryo-EM structure of AIM2-pyd filament in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7K3R
Type: protein
Length: 1,995 residues
Chains: 21
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Interferon-inducible protein AIM2
UniProt: O14862
Pockets: 16 · best druggability 0.86

Structure

electron microscopy · 1 distinct chain · 77% 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, Q, R, S, T, U	Interferon-inducible protein AIM2	protein	95	77% helix, 0% strand	O14862

Pockets

16 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	889	0.86	0.88	88	empty
2	910	0.86	0.88	84	empty
3	888	0.85	0.87	87	empty
4	1007	0.85	0.86	89	empty
5	449	0.80	0.88	44	empty

Interfaces

51 interfaces between chains.

F–L · 528 Å² buried · 5 hydrogen bonds · protein-protein
G–M · 528 Å² buried · 4 hydrogen bonds · protein-protein
H–N · 528 Å² buried · 4 hydrogen bonds · protein-protein
N–T · 526 Å² buried · 4 hydrogen bonds · protein-protein
B–H · 526 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

7K3R · Cryo-EM structure of AIM2-PYD 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 O14862
Elsewhere: RCSB PDB 7K3R · PDBe 7K3R · UniProt O14862

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