Research workbench
Exonuclease domain of lassa virus nucleoprotein bound to manganese
Analyse Exonuclease domain of lassa virus nucleoprotein bound to manganese in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3Q7C
- Type
- protein
- Length
- 209 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nucleoprotein
- UniProt
- P13699
- Ligands
- ZN, MN, PO4
- Pockets
- 2 · best druggability 0.37
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleoprotein | protein | 209 | 37% helix, 17% strand | P13699 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
- MN · Manganese (II) ion · metal · chains A
- PO4 · Phosphate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 118 | 0.37 | 0.74 | 17 | empty |
| 2 | 55 | 0.30 | 0.75 | 16 | PO4 |
Compared structures
- 3Q7C · Exonuclease domain of Lassa virus nucleoprotein bound to manganese · 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 3Q7C · PDBe 3Q7C · UniProt P13699
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