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Structural and functional characterization of human group A rotavirus P[25] VP8*

Analyse Structural and functional characterization of human group A rotavirus P[25] VP8* in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7C8P
Type: protein
Length: 322 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.6
Source: Rotavirus A
Molecule: Outer capsid protein VP4
UniProt: M1GR78
Pockets: 2 · best druggability 0.69

Structure

x-ray diffraction · resolution 2.6 · 1 distinct chain · 8% helix, 56% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Outer capsid protein VP4	protein	161	8% helix, 56% strand	M1GR78

Pockets

2 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	274	0.69	0.84	45	empty
2	168	0.49	0.77	31	empty

Interfaces

1 interface between chains.

A–B · 811 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

7C8P · Structural and functional characterization of human group a rotavirus P[25] VP8* · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt M1GR78
Elsewhere: RCSB PDB 7C8P · PDBe 7C8P · UniProt M1GR78

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