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Pseudoatomic model of the pre-fusion conformation of glycoprotein B of herpes simplex virus 1

Analyse Pseudoatomic model of the pre-fusion conformation of glycoprotein B of herpes… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6Z9M
Type
protein
Length
1,818 residues
Chains
3
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Envelope glycoprotein B
UniProt
A1Z0P7
Pockets
20 · best druggability 0.90

Structure

electron microscopy · 1 distinct chain · 18% helix, 32% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, CEnvelope glycoprotein Bprotein60618% helix, 32% strandA1Z0P7

Pockets

20 pockets found on a 1 Å grid, 17 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19220.900.93148empty
25350.870.9373empty
35260.830.8968empty
410540.820.83104empty
53740.810.9056empty

Interfaces

3 interfaces between chains.

  • A–B · 3578 Ų buried · 76 hydrogen bonds · protein-protein
  • A–C · 3234 Ų buried · 42 hydrogen bonds · protein-protein
  • B–C · 3229 Ų buried · 56 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 disulfide (disulfide).

Compared structures

  • 6Z9M · Pseudoatomic model of the pre-fusion conformation of glycoprotein B of Herpes simplex… · the same entry in another collection · chain A against A, TM-score 1.00

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