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The structure of CVA10 virus a-particle from its complex with Fab 2G8

Analyse The structure of CVA10 virus a-particle from its complex with Fab 2G8 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6ACZ
Type: protein
Length: 652 residues
Chains: 3
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: VP1; VP2; VP3
UniProt: A0A1V0FT21
Pockets: 6 · best druggability 0.76

Structure

electron microscopy · 3 distinct chains · 7% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	VP1	protein	219	5% helix, 25% strand	A0A1V0FT21
B	VP2	protein	213	7% helix, 27% strand	A0A1V0FT21
C	VP3	protein	220	8% helix, 27% strand	A0A1V0FT21

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	434	0.76	0.85	56	empty
2	120	0.52	0.81	24	empty
3	142	0.52	0.80	21	empty
4	65	0.33	0.76	16	empty
5	57	0.32	0.77	15	empty

Interfaces

3 interfaces between chains.

A–C · 3229 Å² buried · 30 hydrogen bonds · protein-protein
A–B · 1608 Å² buried · 21 hydrogen bonds · protein-protein
B–C · 1582 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

6ACZ · The structure of CVA10 virus A-particle from its complex with Fab 2G8 · 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 A0A1V0FT21
Elsewhere: RCSB PDB 6ACZ · PDBe 6ACZ · UniProt A0A1V0FT21

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