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Cryo-EM structures of two intermediates provide insight into adenovirus assembly and disassembly

Analyse Cryo-EM structures of two intermediates provide insight into adenovirus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3ZIF
Type
protein
Length
11,817 residues
Chains
18
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Hexon protein; Penton protein; Pix; Pviii
UniProt
P03278, O71096, Q64845, O92788
Pockets
20 · best druggability 0.89

Structure

electron microscopy · 4 distinct chains · 16% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, LHexon proteinprotein90315% helix, 26% strandP03278
MPenton proteinprotein45011% helix, 26% strandO71096
N, O, P, QPixprotein10736% helix, 0% strandQ64845
RPviiiprotein10327% helix, 5% strandO92788

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111780.890.90149empty
210720.860.87121empty
311900.850.86135empty
48320.850.87102empty
53600.820.9165empty

Interfaces

42 interfaces between chains.

  • J–K · 9051 Ų buried · 150 hydrogen bonds · protein-protein
  • A–B · 9043 Ų buried · 150 hydrogen bonds · protein-protein
  • D–E · 9039 Ų buried · 150 hydrogen bonds · protein-protein
  • G–H · 9030 Ų buried · 150 hydrogen bonds · protein-protein
  • D–F · 9026 Ų buried · 143 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 isopeptide (isopeptide).

Compared structures

  • 3ZIF · Cryo-EM structures of two intermediates provide insight into adenovirus assembly and… · the same entry in another collection · chain A against A, TM-score 1.00

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