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Cryo-EM structure of enterovirus A71 empty particle in complex with Fab h1A6.2

Analyse Cryo-EM structure of enterovirus A71 empty particle in complex with Fab h1A6.2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 8X97
Type: protein
Length: 605 residues
Chains: 3
Method: electron microscopy
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.98
Source: Enterovirus A71
Molecule: Capsid protein VP1; Capsid protein VP2; Capsid protein VP3
UniProt: A0A075QAW4
Pockets: 8 · best druggability 0.62

Structure

electron microscopy · resolution 2.98 · 3 distinct chains · 9% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Capsid protein VP1	protein	204	6% helix, 30% strand	A0A075QAW4
B	Capsid protein VP2	protein	178	11% helix, 43% strand	A0A075QAW4
C	Capsid protein VP3	protein	223	11% helix, 32% strand	A0A075QAW4

Pockets

8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	216	0.62	0.82	33	empty
2	54	0.54	0.89	17	empty
3	138	0.49	0.78	25	empty
4	156	0.48	0.77	30	empty
5	69	0.40	0.80	15	empty

Interfaces

3 interfaces between chains.

A–C · 3019 Å² buried · 33 hydrogen bonds · protein-protein
B–C · 1593 Å² buried · 17 hydrogen bonds · protein-protein
A–B · 1233 Å² buried · 16 hydrogen bonds · protein-protein

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 A0A075QAW4
Elsewhere: RCSB PDB 8X97 · PDBe 8X97 · UniProt A0A075QAW4

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