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Cryo-EM structure of SARS-cov-2 NSP15 nendou at pH 7.5

Analyse Cryo-EM structure of SARS-cov-2 NSP15 nendou at pH 7.5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7RB0
Type
protein
Length
2,082 residues
Chains
6
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Uridylate-specific endoribonuclease
EC
3.1.-.-
UniProt
P0DTD1
Pockets
20 · best druggability 0.88

Structure

electron microscopy · 1 distinct chain · 22% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
D, E, F, A, B, CUridylate-specific endoribonuclease (EC 3.1.-.-)protein34722% helix, 29% strandP0DTD1

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19500.880.89147empty
24470.680.7953empty
34140.670.8053empty
44180.660.7954empty
52600.650.8242empty

Interfaces

15 interfaces between chains.

  • D–F · 1016 Ų buried · 6 hydrogen bonds · protein-protein
  • D–B · 1012 Ų buried · 8 hydrogen bonds · protein-protein
  • A–C · 1009 Ų buried · 8 hydrogen bonds · protein-protein
  • E–A · 1008 Ų buried · 7 hydrogen bonds · protein-protein
  • F–B · 1008 Ų buried · 8 hydrogen bonds · protein-protein

Compared structures

  • 7RB0 · Cryo-EM structure of SARS-CoV-2 NSP15 NendoU at pH 7.5 · the same entry in another collection · chain D against D, TM-score 1.00

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