MolNFT v1 · #184125 · protein + RNA
Lassa virus L protein bound to 3' promoter RNA (well-resolved endonuclease) [3END-endo]
7OEB · RNA-directed RNA polymerase L: “Lassa virus L protein bound to 3' promoter RNA (well-resolved endonuclease) [3END-endo]”. Electron microscopy, 2 ligands (MG, ZN), 20 pockets (best druggability 0.74). MolNFT v1 #184125 on GenesisL1…
- PDB
- 7OEB
- Type
- protein + RNA
- Length
- 1,440 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RNA-directed RNA polymerase L; 3' vrna
- EC
- 2.7.7.48, 3.1.-.-
- UniProt
- A0A3S8NV63
- Ligands
- MG, ZN
- Pockets
- 20 · best druggability 0.74
Structure
electron microscopy · 2 distinct chains · 52% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L | RNA-directed RNA polymerase L (EC 2.7.7.48, 3.1.-.-) | protein | 1434 | 52% helix, 10% strand | A0A3S8NV63 |
| E | 3' vrna | rna | 6 | — | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 918 | 0.74 | 0.78 | 91 | empty |
| 2 | 527 | 0.69 | 0.79 | 57 | empty |
| 3 | 288 | 0.60 | 0.79 | 29 | empty |
| 4 | 125 | 0.55 | 0.82 | 19 | empty |
| 5 | 191 | 0.55 | 0.79 | 28 | empty |
Interfaces
1 interface between chains.
- L–E · 1017 Ų buried · 22 hydrogen bonds · protein-nucleic
Compared structures
- 7OEB · Lassa virus L protein bound to 3' promoter RNA (well-resolved endonuclease) [3END-ENDO] · the same entry in another collection · chain L against L, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt A0A3S8NV63
- Elsewhere: RCSB PDB 7OEB · PDBe 7OEB · UniProt A0A3S8NV63
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