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Cryo-EM structure of an alphavirus, sindbis virus

Analyse Cryo-EM structure of an alphavirus, sindbis virus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6IMM
Type
protein
Length
3,180 residues
Chains
12
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Spike glycoprotein E1; Spike glycoprotein E2; Assembly protein E3
Ligands
8K6
Pockets
20 · best druggability 0.82

Structure

electron microscopy · 3 distinct chains · 12% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
N, T, Z, aSpike glycoprotein E1protein4239% helix, 28% strand—
P, V, d, eSpike glycoprotein E2protein32512% helix, 28% strand—
R, X, h, iAssembly protein E3protein4732% helix, 4% strand—

Ligands and binding sites

  • 8K6 · Octadecane · ligand · chains Z, d

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19420.820.8487empty
210100.800.8177empty
37120.790.8460empty
48750.730.7869empty
53640.710.8251empty

Interfaces

16 interfaces between chains.

  • a–e · 3040 Ų buried · 29 hydrogen bonds · protein-protein
  • Z–d · 2975 Ų buried · 29 hydrogen bonds · protein-protein
  • T–V · 2880 Ų buried · 28 hydrogen bonds · protein-protein
  • N–P · 2746 Ų buried · 22 hydrogen bonds · protein-protein
  • P–R · 510 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

  • 6IMM · Cryo-EM structure of an alphavirus, Sindbis virus · the same entry in another collection · chain N against N, TM-score 1.00

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