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Cryo-EM structure of vaccinia virus scaffolding protein D13 trimer doublet

Analyse Cryo-EM structure of vaccinia virus scaffolding protein D13 trimer doublet in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7VFG
Type
protein
Length
3,162 residues
Chains
6
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Scaffold protein D13
UniProt
P68440
Pockets
20 · best druggability 0.84

Structure

electron microscopy · 1 distinct chain · 17% helix, 41% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
E, F, D, C, A, BScaffold protein D13protein52717% helix, 41% strandP68440

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111840.840.84112empty
29620.830.8496empty
311050.820.83123empty
47090.810.8560empty
56150.800.8564empty

Interfaces

9 interfaces between chains.

  • C–A · 2125 Ų buried · 20 hydrogen bonds · protein-protein
  • E–F · 2121 Ų buried · 20 hydrogen bonds · protein-protein
  • E–D · 2105 Ų buried · 16 hydrogen bonds · protein-protein
  • C–B · 2094 Ų buried · 16 hydrogen bonds · protein-protein
  • A–B · 2049 Ų buried · 20 hydrogen bonds · protein-protein

Compared structures

  • 7VFG · Cryo-EM structure of Vaccinia virus scaffolding protein D13 trimer doublet · the same entry in another collection · chain E against E, TM-score 1.00

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