Research workbench
Structure of np protein from lassa av strain
Analyse Structure of np protein from lassa av strain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3R3L
- Type
- protein
- Length
- 1,537 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nucleoprotein
- UniProt
- Q9DQX7
- Ligands
- MN, ZN
- Pockets
- 20 · best druggability 0.85
Structure
x-ray diffraction · 3 distinct chains · 48% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleoprotein | protein | 513 | 48% helix, 12% strand | Q9DQX7 |
| B | Nucleoprotein | protein | 514 | 49% helix, 11% strand | Q9DQX7 |
| C | Nucleoprotein | protein | 510 | 46% helix, 10% strand | Q9DQX7 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 5 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
20 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1109 | 0.85 | 0.86 | 96 | empty |
| 2 | 1154 | 0.85 | 0.86 | 110 | empty |
| 3 | 980 | 0.84 | 0.85 | 90 | empty |
| 4 | 412 | 0.59 | 0.75 | 50 | empty |
| 5 | 88 | 0.48 | 0.82 | 14 | empty |
Interfaces
2 interfaces between chains.
- A–B · 813 Ų buried · 8 hydrogen bonds · protein-protein
- A–C · 132 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 3R3L · Structure of NP protein from Lassa AV strain · 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 Q9DQX7
- Elsewhere: RCSB PDB 3R3L · PDBe 3R3L · UniProt Q9DQX7
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