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Coxsackievirus B3 Empty particle at pH7.4 (VP3-234Q)

Analyse Coxsackievirus B3 Empty particle at pH7.4 (VP3-234Q) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7VXN
Type: protein
Length: 662 residues
Chains: 3
Method: electron microscopy
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 3.53
Source: Coxsackievirus B3
Molecule: Capsid protein VP1; Capsid protein VP2; Capsid protein VP3
UniProt: P03313
Pockets: 8 · best druggability 0.63

Structure

electron microscopy · resolution 3.53 · 3 distinct chains · 9% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Capsid protein VP1	protein	218	8% helix, 35% strand	P03313
B	Capsid protein VP2	protein	231	9% helix, 32% strand	P03313
C	Capsid protein VP3	protein	213	11% helix, 37% strand	P03313

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	228	0.63	0.82	31	empty
2	116	0.45	0.78	23	empty
3	114	0.44	0.78	20	empty
4	113	0.38	0.74	17	empty
5	127	0.37	0.73	18	empty

Interfaces

3 interfaces between chains.

A–C · 2703 Å² buried · 32 hydrogen bonds · protein-protein
A–B · 1850 Å² buried · 24 hydrogen bonds · protein-protein
B–C · 1498 Å² buried · 13 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 P03313
Elsewhere: RCSB PDB 7VXN · PDBe 7VXN · UniProt P03313

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