MolNFT v1 · #142709 · protein

The structure of CVA10 virus a-particle

6ACY · VP1: “The structure of CVA10 virus a-particle”. Electron microscopy, 7 pockets (best druggability 0.73). MolNFT v1 #142709 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6ACY
Type: protein
Length: 651 residues
Chains: 3
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: VP1; VP2; VP3
UniProt: A0A1V0FT21
Pockets: 7 · best druggability 0.73

Structure

electron microscopy · 3 distinct chains · 8% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	VP1	protein	223	6% helix, 25% strand	A0A1V0FT21
B	VP2	protein	213	11% helix, 35% strand	A0A1V0FT21
C	VP3	protein	215	6% helix, 31% strand	A0A1V0FT21

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	270	0.73	0.86	44	empty
2	125	0.50	0.80	22	empty
3	84	0.46	0.81	19	empty
4	85	0.46	0.81	20	empty
5	168	0.42	0.73	28	empty

Interfaces

3 interfaces between chains.

A–C · 3061 Å² buried · 37 hydrogen bonds · protein-protein
A–B · 1652 Å² buried · 22 hydrogen bonds · protein-protein
B–C · 1564 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

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

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