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Structure of the west nile virus envelope glycoprotein

Analyse Structure of the west nile virus envelope glycoprotein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2HG0
Type: protein
Length: 400 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Envelope glycoprotein
UniProt: Q3I0Y8
Ligands: NAG, NDG, FUL
Pockets: 6 · best druggability 0.58

Structure

x-ray diffraction · 1 distinct chain · 8% helix, 41% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Envelope glycoprotein	protein	400	8% helix, 41% strand	Q3I0Y8

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
NDG · 2-acetamido-2-deoxy-alpha-D-glucopyranose · sugar
FUL · beta-L-fucopyranose · sugar · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	166	0.58	0.82	28	empty
2	66	0.50	0.85	18	empty
3	50	0.44	0.83	12	empty
4	79	0.36	0.76	18	empty
5	103	0.35	0.74	19	empty

Modifications

Observed in the structure: 6 disulfide, 1 glycan (disulfide, N-glycosylation).

Compared structures

2HG0 · Structure of the West Nile Virus envelope glycoprotein · 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 Q3I0Y8
Elsewhere: RCSB PDB 2HG0 · PDBe 2HG0 · UniProt Q3I0Y8

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