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Mapping the E2 glycoprotein of alphaviruses

Analyse Mapping the E2 glycoprotein of alphaviruses in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1Z8Y
Type
protein
Length
2,388 residues
Chains
20
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Spike glycoprotein E1; Spike glycoprotein E2; Capsid protein C
EC
3.4.21.-
UniProt
P03316, P11259
Pockets
19 · best druggability 0.61

Structure

electron microscopy · 5 distinct chains · 11% helix, 32% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, C, E, GSpike glycoprotein E1protein2906% helix, 31% strandP03316
B, D, F, HSpike glycoprotein E1protein890% helix, 31% strandP03316
I, K, M, OSpike glycoprotein E1protein3126% helix, 0% strandP03316
J, L, N, PSpike glycoprotein E2protein3686% helix, 0% strandP11259
Q, R, S, TCapsid protein C (EC 3.4.21.-)protein1516% helix, 48% strandP03316

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1510.610.9325empty
2880.570.8619empty
32360.560.7841empty
41410.530.8127empty
5930.510.8322empty

Interfaces

19 interfaces between chains.

  • C–D · 566 Ų buried · 7 hydrogen bonds · protein-protein
  • E–F · 523 Ų buried · 9 hydrogen bonds · protein-protein
  • A–B · 456 Ų buried · 9 hydrogen bonds · protein-protein
  • M–N · 408 Ų buried · 0 hydrogen bonds · protein-protein
  • K–L · 407 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 32 disulfide (disulfide).

Compared structures

  • 1Z8Y · Mapping the E2 Glycoprotein of Alphaviruses · the same entry in another collection · chain J against J, TM-score 1.00

Analyse

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