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Crystal Structure of NendoU (Uridylate-specific endoribonuclease, nsp15) from Betacoronavirus SARS-CoV-2

Analyse Crystal Structure of NendoU (Uridylate-specific endoribonuclease, nsp15) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6XDH
Type
protein
Length
696 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.35
Source
Severe acute respiratory syndrome coronavirus 2
Molecule
Uridylate-specific endoribonuclease
EC
3.1.-.-
UniProt
P0DTD1
Pockets
7 · best druggability 0.59

Structure

x-ray diffraction · resolution 2.35 · 2 distinct chains · 22% helix, 31% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AUridylate-specific endoribonuclease (EC 3.1.-.-)protein34721% helix, 31% strandP0DTD1
BUridylate-specific endoribonuclease (EC 3.1.-.-)protein34922% helix, 31% strandP0DTD1

Ligands and binding sites

  • FMT · Formic acid · additive · 5 copies · chains A, B
  • ACT · Acetate ion · additive · 3 copies · chains A, B
  • CIT · Citric acid · additive · 2 copies · chains A, B
  • EDO · 1,2-ethanediol · additive · chains B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12400.590.8030empty
21910.570.8029empty
3620.340.7714empty
4780.320.7416empty
5700.320.7519empty

Interfaces

1 interface between chains.

  • A–B · 600 Ų buried · 6 hydrogen bonds · protein-protein

Compared structures

  • 6XDH · Crystal structure of nendou (uridylate-specific endoribonuclease, NSP15) from… · the same entry in another collection · chain A against A, TM-score 1.00

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