MolNFT v2 · #215610 · protein

Cryo-EM reconstruction of VP4 assembly from SA11 Rotavirus Non-Tripsinized Triple Layered Particle

8OLE · Outer capsid protein VP4: “Cryo-EM reconstruction of VP4 assembly from SA11 Rotavirus Non-Tripsinized Triple Layered Particle”. Electron microscopy at 4.4, 20 pockets (best druggability 0.88). MolNFT v2 #215610 on GenesisL1: 3D…

PDB: 8OLE
Type: protein
Length: 2,254 residues
Chains: 3
Method: electron microscopy
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 4.4
Source: Rotavirus
Molecule: Outer capsid protein VP4
UniProt: A0A060IEP4
Pockets: 20 · best druggability 0.88

Structure

electron microscopy · resolution 4.4 · 2 distinct chains · 24% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
X, Y	Outer capsid protein VP4	protein	776	24% helix, 23% strand	A0A060IEP4
Z	Outer capsid protein VP4	protein	702	24% helix, 25% strand	A0A060IEP4

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1125	0.88	0.89	141	empty
2	327	0.82	0.91	62	empty
3	402	0.78	0.87	58	empty
4	93	0.78	0.98	26	empty
5	75	0.76	0.98	23	empty

Interfaces

3 interfaces between chains.

X–Y · 6774 Å² buried · 128 hydrogen bonds · protein-protein
Y–Z · 3082 Å² buried · 44 hydrogen bonds · protein-protein
X–Z · 1738 Å² buried · 15 hydrogen bonds · protein-protein

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 A0A060IEP4
Elsewhere: RCSB PDB 8OLE · PDBe 8OLE · UniProt A0A060IEP4

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