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MolNFT v1 · #84360 · protein

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

3ZIF · Hexon protein: “Cryo-EM structures of two intermediates provide insight into adenovirus assembly and disassembly”. Electron microscopy, 20 pockets (best druggability 0.89). MolNFT v1 #84360 on GenesisL1: 3D structure, binding sites…

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

Analyse

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