MolNFT v1 · #142707 · protein

The structure of CVA10 virus procapsid particle

6ACW · VP1: “The structure of CVA10 virus procapsid particle”. Electron microscopy, 7 pockets (best druggability 0.70). MolNFT v1 #142707 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6ACW
Type: protein
Length: 614 residues
Chains: 3
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: VP1; VP0; VP3
UniProt: A0A1V0FT21
Pockets: 7 · best druggability 0.70

Structure

electron microscopy · 3 distinct chains · 8% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	VP1	protein	201	7% helix, 27% strand	A0A1V0FT21
B	VP0	protein	199	8% helix, 31% strand	A0A1V0FT21
C	VP3	protein	214	9% helix, 27% strand	A0A1V0FT21

Pockets

7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	352	0.70	0.83	39	empty
2	104	0.54	0.84	19	empty
3	132	0.54	0.81	20	empty
4	159	0.51	0.79	26	empty
5	98	0.42	0.78	25	empty

Interfaces

3 interfaces between chains.

A–C · 2557 Å² buried · 36 hydrogen bonds · protein-protein
A–B · 1596 Å² buried · 16 hydrogen bonds · protein-protein
B–C · 1556 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

6ACW · The structure of CVA10 virus procapsid 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 A0A1V0FT21
Elsewhere: RCSB PDB 6ACW · PDBe 6ACW · UniProt A0A1V0FT21

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