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Cryo-EM structure of the apo NSP12-NSP7-NSP8 complex

Analyse Cryo-EM structure of the apo NSP12-NSP7-NSP8 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7BV1
Type
protein
Length
1,112 residues
Chains
4
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
RNA-directed RNA polymerase; Non-structural protein 8; Non-structural protein 7
EC
2.7.7.48
UniProt
P0DTD1
Ligands
ZN
Pockets
15 · best druggability 0.64

Structure

electron microscopy · 4 distinct chains · 43% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARNA-directed RNA polymerase (EC 2.7.7.48)protein83643% helix, 15% strandP0DTD1
BNon-structural protein 8protein11439% helix, 26% strandP0DTD1
CNon-structural protein 7protein6376% helix, 0% strandP0DTD1
DNon-structural protein 8protein9925% helix, 20% strandP0DTD1

Ligands and binding sites

  • ZN · Zinc ion · metal · 2 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13570.640.7942empty
23650.560.7533empty
31640.560.8132empty
42000.530.7830empty
5620.530.8726empty

Interfaces

5 interfaces between chains.

  • A–B · 2361 Ų buried · 12 hydrogen bonds · protein-protein
  • C–D · 975 Ų buried · 4 hydrogen bonds · protein-protein
  • A–C · 799 Ų buried · 6 hydrogen bonds · protein-protein
  • B–C · 157 Ų buried · 3 hydrogen bonds · protein-protein
  • A–D · 144 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 7BV1 · Cryo-EM structure of the apo nsp12-nsp7-nsp8 complex · the same entry in another collection · chain A against A, TM-score 1.00

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