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Bat influenza a polymerase pre-initiation complex

Analyse Bat influenza a polymerase pre-initiation complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6T0N
Type
protein + RNA
Length
1,731 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
2.7.7.48
UniProt
H6QM92, H6QM91, H6QM90
Ligands
MG
Pockets
20 · best druggability 0.86

Structure

electron microscopy · 5 distinct chains · 44% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APolymerase acidic proteinprotein70442% helix, 18% strandH6QM92
BRNA-directed RNA polymerase catalytic subunit (EC 2.7.7.48)protein74947% helix, 16% strandH6QM91
CPolymerase basic protein 2protein25042% helix, 17% strandH6QM90
V5' vrnarna14——
R3' vrnarna14——

Ligands and binding sites

  • MG · Magnesium ion · metal · 2 copies · chains B, A, V

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18820.860.88104empty
211740.820.8492empty
39820.780.8065empty
48280.770.8173empty
5840.750.9722empty

Interfaces

9 interfaces between chains.

  • A–B · 8997 Ų buried · 144 hydrogen bonds · protein-protein
  • B–C · 6666 Ų buried · 70 hydrogen bonds · protein-protein
  • A–V · 1340 Ų buried · 24 hydrogen bonds · protein-nucleic
  • A–C · 1282 Ų buried · 8 hydrogen bonds · protein-protein
  • B–R · 1132 Ų buried · 29 hydrogen bonds · protein-nucleic

Compared structures

  • 6T0N · Bat Influenza A polymerase pre-initiation complex · the same entry in another collection · chain A against A, TM-score 1.00

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