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

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

PDB
7VFH
Type
protein
Length
9,486 residues
Chains
18
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Scaffold protein D13
UniProt
P68440
Pockets
20 · best druggability 0.85

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, L, J, K, N, O, M, Q, R, PScaffold 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
19190.850.8697empty
210100.840.85100empty
310680.840.8595empty
411410.840.85111empty
511350.840.85100empty

Interfaces

36 interfaces between chains.

  • N–O · 2157 Ų buried · 16 hydrogen bonds · protein-protein
  • G–I · 2151 Ų buried · 18 hydrogen bonds · protein-protein
  • E–F · 2146 Ų buried · 17 hydrogen bonds · protein-protein
  • J–K · 2143 Ų buried · 19 hydrogen bonds · protein-protein
  • R–P · 2143 Ų buried · 19 hydrogen bonds · protein-protein

Compared structures

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

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