Research workbench
Lassa fever virus nucleoprotein complexed with UTP
Analyse Lassa fever virus nucleoprotein complexed with UTP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3MX5
- Type
- protein
- Length
- 1,543 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nucleoprotein
- UniProt
- P13699
- Ligands
- UTP, ZN
- Pockets
- 19 · best druggability 0.83
Structure
x-ray diffraction · 3 distinct chains · 50% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleoprotein | protein | 516 | 51% helix, 11% strand | P13699 |
| B | Nucleoprotein | protein | 515 | 50% helix, 12% strand | P13699 |
| C | Nucleoprotein | protein | 512 | 50% helix, 12% strand | P13699 |
Ligands and binding sites
- UTP · Uridine 5'-triphosphate · ligand · 3 copies · chains A, B, C
- ZN · Zinc ion · metal · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
19 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 997 | 0.83 | 0.84 | 80 | UTP |
| 2 | 1145 | 0.83 | 0.84 | 89 | UTP |
| 3 | 1193 | 0.82 | 0.83 | 88 | UTP |
| 4 | 486 | 0.61 | 0.75 | 65 | empty |
| 5 | 98 | 0.50 | 0.82 | 15 | empty |
Interfaces
2 interfaces between chains.
- A–B · 653 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 145 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 3MX5 · Lassa fever virus nucleoprotein complexed with UTP · 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 3MX5 · PDBe 3MX5 · UniProt P13699
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