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Structural basis of glycan recognition in neonate-specific rotaviruses

Analyse Structural basis of glycan recognition in neonate-specific rotaviruses in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4YFW
Type: protein
Length: 322 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Outer capsid protein VP4
UniProt: B6RGK2
Pockets: 1 · best druggability 0.60

Structure

x-ray diffraction · 1 distinct chain · 8% helix, 52% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Outer capsid protein VP4	protein	161	8% helix, 52% strand	B6RGK2

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	157	0.60	0.83	29	empty

Interfaces

1 interface between chains.

A–B · 475 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

4YFW · Structural basis of glycan recognition in neonate-specific rotaviruses · 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 B6RGK2
Elsewhere: RCSB PDB 4YFW · PDBe 4YFW · UniProt B6RGK2

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