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MolNFT v1 · #167463 · protein

A varicella-zoster virus glycoprotein

6VLK · Envelope glycoprotein B: “A varicella-zoster virus glycoprotein”. X-ray diffraction, 3 ligands (NAG, MAN, BMA), 11 pockets (best druggability 0.51). MolNFT v1 #167463 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB
6VLK
Type
protein
Length
1,167 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Envelope glycoprotein B
UniProt
Q4JR05
Ligands
NAG, MAN, BMA
Pockets
11 · best druggability 0.51

Structure

x-ray diffraction · 2 distinct chains · 20% helix, 38% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AEnvelope glycoprotein Bprotein58420% helix, 38% strandQ4JR05
BEnvelope glycoprotein Bprotein58320% helix, 38% strandQ4JR05

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 9 copies · chains A, B
  • MAN · alpha-D-mannopyranose · sugar · 6 copies · chains A
  • BMA · beta-D-mannopyranose · sugar · 2 copies

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11990.510.7728empty
21820.480.7621empty
31530.450.7621empty
41140.450.7832empty
51440.440.7622empty

Interfaces

1 interface between chains.

  • A–B · 341 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 disulfide, 6 glycan (disulfide, N-glycosylation).

Compared structures

  • 6VLK · A varicella-zoster virus glycoprotein · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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