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The structure of CVA10 procapsid from its complex with Fab 2G8

Analyse The structure of CVA10 procapsid 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: 6AD1
Type: protein
Length: 637 residues
Chains: 3
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: VP1; VP0; VP3
UniProt: A0A1V0FT21
Pockets: 8 · best druggability 0.70

Structure

electron microscopy · 3 distinct chains · 6% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	VP1	protein	211	6% helix, 24% strand	A0A1V0FT21
B	VP0	protein	207	6% helix, 26% strand	A0A1V0FT21
C	VP3	protein	219	6% helix, 23% strand	A0A1V0FT21

Pockets

8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	261	0.70	0.85	32	empty
2	224	0.69	0.86	32	empty
3	159	0.55	0.80	24	empty
4	98	0.54	0.84	18	empty
5	105	0.53	0.83	19	empty

Interfaces

3 interfaces between chains.

A–C · 2754 Å² buried · 22 hydrogen bonds · protein-protein
A–B · 1750 Å² buried · 24 hydrogen bonds · protein-protein
B–C · 1592 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

6AD1 · The structure of CVA10 procapsid 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 6AD1 · PDBe 6AD1 · UniProt A0A1V0FT21

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