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Cryo-EM structure of the respiratory syncytial virus polymerase (L) protein bound by the tetrameric phosphoprotein (P)

Analyse Cryo-EM structure of the respiratory syncytial virus polymerase (L) protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6PZK
Type
protein
Length
1,624 residues
Chains
5
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
RNA-directed RNA polymerase L; Phosphoprotein
EC
2.7.7.48, 2.1.1.56, 2.7.7.-, 2.7.7.88
UniProt
P28887, P03421
Pockets
20 · best druggability 0.79

Structure

electron microscopy · 5 distinct chains · 56% helix, 8% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARNA-directed RNA polymerase L (EC 2.7.7.48, 2.1.1.56, 2.7.7.-, 2.7.7.88)protein136153% helix, 9% strandP28887
BPhosphoproteinprotein9855% helix, 12% strandP03421
CPhosphoproteinprotein5777% helix, 0% strandP03421
DPhosphoproteinprotein5585% helix, 0% strandP03421
EPhosphoproteinprotein5389% helix, 0% strandP03421

Pockets

20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111940.790.81115empty
210590.770.7972empty
36640.690.7768empty
42820.620.8045empty
51650.580.8233empty

Interfaces

10 interfaces between chains.

  • A–B · 2170 Ų buried · 43 hydrogen bonds · protein-protein
  • A–C · 1758 Ų buried · 28 hydrogen bonds · protein-protein
  • C–D · 1312 Ų buried · 10 hydrogen bonds · protein-protein
  • D–E · 1284 Ų buried · 5 hydrogen bonds · protein-protein
  • B–C · 805 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

  • 6PZK · Cryo-EM Structure of the Respiratory Syncytial Virus Polymerase (L) Protein Bound by the… · the same entry in another collection · chain A against A, TM-score 1.00

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