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Lassa virus L protein in a pre-initiation conformation [preinitiation]

Analyse Lassa virus L protein in a pre-initiation conformation [preinitiation] in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7OJL
Type
protein + RNA
Length
1,531 residues
Chains
3
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
RNA-directed RNA polymerase L; 3' RNA; 5' RNA
EC
2.7.7.48, 3.1.-.-
UniProt
A0A3S8NV63
Ligands
MN
Pockets
18 · best druggability 0.75

Structure

electron microscopy · 3 distinct chains · 50% helix, 8% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
LRNA-directed RNA polymerase L (EC 2.7.7.48, 3.1.-.-)protein149850% helix, 8% strandA0A3S8NV63
E3' RNArna13——
D5' RNArna20——

Ligands and binding sites

  • MN · Manganese (II) ion · metal · chains L

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

Pockets

18 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110010.750.7871empty
27880.730.7981empty
37860.730.7876empty
49450.730.7772empty
54100.680.8050empty

Interfaces

3 interfaces between chains.

  • L–D · 2059 Ų buried · 38 hydrogen bonds · protein-nucleic
  • L–E · 1305 Ų buried · 38 hydrogen bonds · protein-nucleic
  • E–D · 432 Ų buried · 29 hydrogen bonds · nucleic-nucleic

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 7OJL · Lassa virus L protein in a pre-initiation conformation [PREINITIATION] · the same entry in another collection · chain D against D, TM-score 1.00

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