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Crystal structure of Ebinur Lake virus cap snatching endonuclease (WT)

Analyse Crystal structure of Ebinur Lake virus cap snatching endonuclease (WT) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7EWU
Type
protein
Length
721 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.11
Source
Abbey lake orthobunyavirus
Molecule
Replicase
EC
2.7.7.48
UniProt
A0A059WLS9
Ligands
MN
Pockets
6 · best druggability 0.57

Structure

x-ray diffraction · resolution 2.11 · 3 distinct chains · 52% helix, 14% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AReplicase (EC 2.7.7.48)protein18051% helix, 13% strandA0A059WLS9
B, CReplicase (EC 2.7.7.48)protein18153% helix, 13% strandA0A059WLS9
DReplicase (EC 2.7.7.48)protein17953% helix, 15% strandA0A059WLS9

Ligands and binding sites

  • MN · Manganese (II) ion · metal · 6 copies · chains B, C, D

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

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13390.570.7633empty
21710.560.8029empty
32540.520.7528empty
41380.420.7520empty
5780.330.7512empty

Interfaces

5 interfaces between chains.

  • A–D · 480 Ų buried · 2 hydrogen bonds · protein-protein
  • B–C · 391 Ų buried · 1 hydrogen bond · protein-protein
  • B–D · 251 Ų buried · 2 hydrogen bonds · protein-protein
  • A–B · 58 Ų buried · 0 hydrogen bonds · protein-protein
  • A–C · 11 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 7EWU · Crystal structure of ebinur lake virus cap snatching endonuclease (wt) · the same entry in another collection · chain A against A, TM-score 1.00

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