Research workbench
Cryoem structure of the nipah virus nucleocapsid single helical turn assembly
Analyse Cryoem structure of the nipah virus nucleocapsid single helical turn assembly in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7NT5
- Type
- protein + RNA
- Length
- 5,196 residues
- Chains
- 14
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nucleoprotein; RNA (78-mer)
- UniProt
- Q9IK92
- Pockets
- 20 · best druggability 0.86
Structure
electron microscopy · 5 distinct chains · 61% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Nucleoprotein | protein | 394 | 62% helix, 4% strand | Q9IK92 |
| B, D, E, F, G, H, I, J, K | Nucleoprotein | protein | 395 | 60% helix, 5% strand | Q9IK92 |
| L | Nucleoprotein | protein | 393 | 60% helix, 5% strand | Q9IK92 |
| M | Nucleoprotein | protein | 382 | 62% helix, 4% strand | Q9IK92 |
| N | RNA (78-mer) | rna | 78 | — | — |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 443 | 0.86 | 0.94 | 71 | empty |
| 2 | 436 | 0.86 | 0.94 | 59 | empty |
| 3 | 422 | 0.85 | 0.93 | 56 | empty |
| 4 | 413 | 0.85 | 0.93 | 60 | empty |
| 5 | 419 | 0.85 | 0.93 | 54 | empty |
Interfaces
35 interfaces between chains.
- I–J · 3079 Ų buried · 22 hydrogen bonds · protein-protein
- D–E · 3072 Ų buried · 35 hydrogen bonds · protein-protein
- E–F · 3034 Ų buried · 30 hydrogen bonds · protein-protein
- C–D · 3013 Ų buried · 30 hydrogen bonds · protein-protein
- G–H · 2995 Ų buried · 31 hydrogen bonds · protein-protein
Compared structures
- 7NT5 · CryoEM structure of the Nipah virus nucleocapsid single helical turn assembly · 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 Q9IK92
- Elsewhere: RCSB PDB 7NT5 · PDBe 7NT5 · UniProt Q9IK92
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