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Crystal structure of NSP15 endoribonuclease from SARS cov-2 in the complex with uridine-5'-monophosphate

Analyse Crystal structure of NSP15 endoribonuclease from SARS cov-2 in the complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6WLC
Type
protein
Length
696 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Uridylate-specific endoribonuclease
EC
3.1.-.-
UniProt
P0DTD1
Ligands
U5P, SO4
Pockets
5 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 21% helix, 31% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BUridylate-specific endoribonuclease (EC 3.1.-.-)protein34821% helix, 31% strandP0DTD1

Ligands and binding sites

  • U5P · Uridine-5'-monophosphate · ligand · 2 copies · chains A, B
  • SO4 · Sulfate ion · ion · chains A
  • EDO · 1,2-ethanediol · additive · 10 copies · chains A, B
  • ACT · Acetate ion · additive · 4 copies · chains A, B
  • TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 2 copies · chains A, B
  • FMT · Formic acid · additive · 2 copies · chains B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12510.590.7934empty
22190.580.8025EDO
31640.410.7228empty
4980.370.7519empty
5600.270.7317empty

Interfaces

1 interface between chains.

  • A–B · 30 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 6WLC · Crystal Structure of NSP15 Endoribonuclease from SARS CoV-2 in the Complex with… · the same entry in another collection · chain A against A, TM-score 1.00

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