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Crystal structure of the oligomerization domain of VP35 from reston virus, mercury derivative

Analyse Crystal structure of the oligomerization domain of VP35 from reston virus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6GBR
Type
protein
Length
270 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Polymerase cofactor VP35
UniProt
Q8JPY0
Ligands
MBO
Pockets
2 · best druggability 0.57

Structure

x-ray diffraction · 4 distinct chains · 93% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APolymerase cofactor VP35protein6796% helix, 0% strandQ8JPY0
BPolymerase cofactor VP35protein6692% helix, 0% strandQ8JPY0
CPolymerase cofactor VP35protein7093% helix, 0% strandQ8JPY0
DPolymerase cofactor VP35protein6793% helix, 0% strandQ8JPY0

Ligands and binding sites

  • MBO · Mercuribenzoic acid · ligand · 2 copies · chains A, B, C, D

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11000.570.8513empty
2650.410.8011empty

Interfaces

6 interfaces between chains.

  • A–D · 1647 Ų buried · 6 hydrogen bonds · protein-protein
  • B–C · 1615 Ų buried · 10 hydrogen bonds · protein-protein
  • C–D · 1253 Ų buried · 8 hydrogen bonds · protein-protein
  • A–B · 1203 Ų buried · 8 hydrogen bonds · protein-protein
  • A–C · 573 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

  • 6GBR · Crystal Structure of the oligomerization domain of VP35 from Reston virus, mercury… · the same entry in another collection · chain A against A, TM-score 1.00

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