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1918 H1N1 viral influenza polymerase heterotrimer with NB8199 core

Analyse 1918 H1N1 viral influenza polymerase heterotrimer with NB8199 core in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7NJ5
Type
protein + RNA
Length
1,823 residues
Chains
6
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Polymerase acidic protein; RNA-directed RNA polymerase catalytic subunit; Polymerase…
EC
3.1.-.-, 2.7.7.48
UniProt
Q3HM39, Q3HM40, Q3HM41
Pockets
20 · best druggability 0.84

Structure

electron microscopy · 6 distinct chains · 42% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APolymerase acidic protein (EC 3.1.-.-)protein71642% helix, 16% strandQ3HM39
BRNA-directed RNA polymerase catalytic subunit (EC 2.7.7.48)protein73547% helix, 15% strandQ3HM40
CPolymerase basic protein 2,IMMUNOGLOBULIN G-binding protein aprotein24943% helix, 17% strandQ3HM41
ERNA (5'-R(P*GP*GP*CP*CP*UP*GP*CP*U)-3')rna8——
DRNA (5'-R(P*AP*GP*UP*AP*GP*AP*AP*AP*CP*AP*AP*GP*GP*CP*C)- 3')rna15——
FNB8199 coreprotein1003% helix, 54% strand—

Pockets

20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17170.840.8891empty
28170.820.8576empty
36220.810.8660empty
49880.790.81111empty
53000.760.8857empty

Interfaces

9 interfaces between chains.

  • A–B · 8941 Ų buried · 106 hydrogen bonds · protein-protein
  • B–C · 6785 Ų buried · 53 hydrogen bonds · protein-protein
  • A–D · 1396 Ų buried · 20 hydrogen bonds · protein-nucleic
  • A–C · 1321 Ų buried · 10 hydrogen bonds · protein-protein
  • B–D · 626 Ų buried · 6 hydrogen bonds · protein-nucleic

Compared structures

  • 7NJ5 · 1918 H1N1 Viral influenza polymerase heterotrimer with Nb8199 core · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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