Research workbench
Mopeia virus exonuclease domain complexed with magnesium
Analyse Mopeia virus exonuclease domain complexed with magnesium in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5LRP
- Type
- protein
- Length
- 412 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nucleoprotein
- UniProt
- Q5S581
- Ligands
- ZN, MG
- Pockets
- 6 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Nucleoprotein | protein | 206 | 37% helix, 19% strand | Q5S581 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 303 | 0.63 | 0.80 | 39 | empty |
| 2 | 189 | 0.47 | 0.75 | 24 | empty |
| 3 | 80 | 0.47 | 0.82 | 15 | empty |
| 4 | 140 | 0.42 | 0.75 | 22 | empty |
| 5 | 91 | 0.39 | 0.76 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 344 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 5LRP · Mopeia Virus Exonuclease domain complexed with Magnesium · 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 Q5S581
- Elsewhere: RCSB PDB 5LRP · PDBe 5LRP · UniProt Q5S581
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.