MolNFT v1 · #177190 · protein

ECHOVIRUS3 empty expanded particle

7EAH · Capsid protein VP1: “ECHOVIRUS3 empty expanded particle”. Electron microscopy, 9 pockets (best druggability 0.70). MolNFT v1 #177190 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7EAH
Type: protein
Length: 710 residues
Chains: 3
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Capsid protein VP1; Capsid protein VP0; Capsid protein VP3
UniProt: A0A6M4MJE3
Pockets: 9 · best druggability 0.70

Structure

electron microscopy · 3 distinct chains · 9% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
1	Capsid protein VP1	protein	231	8% helix, 33% strand	A0A6M4MJE3
2	Capsid protein VP0	protein	250	11% helix, 34% strand	A0A6M4MJE3
3	Capsid protein VP3	protein	229	9% helix, 33% strand	A0A6M4MJE3

Pockets

9 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	153	0.70	0.89	31	empty
2	210	0.54	0.78	39	empty
3	75	0.50	0.84	23	empty
4	135	0.44	0.76	21	empty
5	92	0.43	0.79	17	empty

Interfaces

3 interfaces between chains.

1–3 · 3555 Å² buried · 46 hydrogen bonds · protein-protein
1–2 · 1875 Å² buried · 21 hydrogen bonds · protein-protein
2–3 · 1536 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

7EAH · Echovirus3 empty expanded particle · the same entry in another collection · chain 1 against 1, 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 A0A6M4MJE3
Elsewhere: RCSB PDB 7EAH · PDBe 7EAH · UniProt A0A6M4MJE3

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