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Cryo-EM structure of SARS-cov-2 NSP15 nendou in bis-tris pH 6.0

Analyse Cryo-EM structure of SARS-cov-2 NSP15 nendou in bis-tris pH 6.0 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7RB2
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 0.84

Structure

electron microscopy · 1 distinct chain · 21% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, FUridylate-specific endoribonuclease (EC 3.1.-.-)protein34721% 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
18150.840.87104empty
25360.700.7960empty
34880.700.8052empty
45190.700.7960empty
54960.690.7957empty

Interfaces

15 interfaces between chains.

  • B–F · 1058 Ų buried · 6 hydrogen bonds · protein-protein
  • B–C · 1046 Ų buried · 8 hydrogen bonds · protein-protein
  • C–F · 1045 Ų buried · 6 hydrogen bonds · protein-protein
  • A–E · 1040 Ų buried · 7 hydrogen bonds · protein-protein
  • A–D · 1037 Ų buried · 7 hydrogen bonds · protein-protein

Compared structures

  • 7RB2 · Cryo-EM structure of SARS-CoV-2 NSP15 NendoU in BIS-Tris pH 6.0 · the same entry in another collection · chain A against A, TM-score 1.00

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