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Cryoem structure of human enterovirus 70 a-particle

Analyse Cryoem structure of human enterovirus 70 a-particle in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7OZI
Type: protein
Length: 661 residues
Chains: 3
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Capsid protein VP1; Capsid protein VP2; Capsid protein VP3
UniProt: P32537
Pockets: 7 · best druggability 0.62

Structure

electron microscopy · 3 distinct chains · 10% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Capsid protein VP1	protein	221	6% helix, 36% strand	P32537
B	Capsid protein VP2	protein	218	12% helix, 31% strand	P32537
C	Capsid protein VP3	protein	222	11% helix, 33% strand	P32537

Pockets

7 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	129	0.62	0.86	24	empty
2	167	0.47	0.76	28	empty
3	122	0.44	0.77	21	empty
4	115	0.40	0.76	22	empty
5	71	0.37	0.77	15	empty

Interfaces

3 interfaces between chains.

A–C · 3014 Å² buried · 35 hydrogen bonds · protein-protein
A–B · 1795 Å² buried · 37 hydrogen bonds · protein-protein
B–C · 1581 Å² buried · 19 hydrogen bonds · protein-protein

Compared structures

7OZI · CryoEM structure of human enterovirus 70 A-particle · the same entry in another collection · chain A against A, 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 P32537
Elsewhere: RCSB PDB 7OZI · PDBe 7OZI · UniProt P32537

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