Research workbench
Structural basis for the dsrna specificity of the lassa virus np exonuclease
Analyse Structural basis for the dsrna specificity of the lassa virus np exonuclease in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4FVU
- Type
- protein + RNA
- Length
- 224 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nucleoprotein; RNA (5'-R(*GP*GP*AP*GP*GP*GP*AP*G)-3'); RNA…
- UniProt
- P13699
- Ligands
- ZN, MG
- Pockets
- 3 · best druggability 0.47
Structure
x-ray diffraction · 3 distinct chains · 39% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleoprotein | protein | 208 | 39% helix, 20% strand | P13699 |
| B | RNA (5'-R(*GP*GP*AP*GP*GP*GP*AP*G)-3') | rna | 8 | — | — |
| C | RNA (5'-R(*CP*UP*CP*CP*CP*UP*CP*C)-3') | rna | 8 | — | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 125 | 0.47 | 0.79 | 21 | empty |
| 2 | 158 | 0.44 | 0.76 | 17 | empty |
| 3 | 78 | 0.34 | 0.75 | 17 | empty |
Interfaces
3 interfaces between chains.
- A–B · 443 Ų buried · 12 hydrogen bonds · protein-nucleic
- B–C · 387 Ų buried · 49 hydrogen bonds · nucleic-nucleic
- A–C · 250 Ų buried · 5 hydrogen bonds · protein-nucleic
Compared structures
- 4FVU · Structural basis for the dsRNA specificity of the Lassa virus NP exonuclease · the same entry in another collection · chain A against A, 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 P13699
- Elsewhere: RCSB PDB 4FVU · PDBe 4FVU · UniProt P13699
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