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1918 H1N1 viral influenza polymerase heterotrimer - endonuclease ordered (CLASS2B)

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

PDB
7NHC
Type
protein + RNA
Length
1,703 residues
Chains
5
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 0.80

Structure

electron microscopy · 5 distinct chains · 46% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APolymerase acidic protein (EC 3.1.-.-)protein71643% helix, 17% strandQ3HM39
BRNA-directed RNA polymerase catalytic subunit (EC 2.7.7.48)protein71748% helix, 14% strandQ3HM40
CPolymerase basic protein 2,IMMUNOGLOBULIN G-binding protein aprotein24745% 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——

Pockets

20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15340.800.8750empty
210910.740.7790empty
310520.730.7760empty
4570.730.9918empty
52580.730.8733empty

Interfaces

9 interfaces between chains.

  • A–B · 9114 Ų buried · 124 hydrogen bonds · protein-protein
  • B–C · 6280 Ų buried · 68 hydrogen bonds · protein-protein
  • A–D · 1364 Ų buried · 21 hydrogen bonds · protein-nucleic
  • A–C · 1360 Ų buried · 11 hydrogen bonds · protein-protein
  • B–D · 640 Ų buried · 9 hydrogen bonds · protein-nucleic

Compared structures

  • 7NHC · 1918 H1N1 Viral influenza polymerase heterotrimer - Endonuclease ordered (Class2b) · the same entry in another collection · chain A against A, TM-score 1.00

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