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The coiled-coil domain (residues 1-93) structure of the sin nombre virus nucleocapsid protein
Analyse The coiled-coil domain (residues 1-93) structure of the sin nombre virus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2IC9
- Type
- protein
- Length
- 145 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nucleocapsid protein
- UniProt
- Q81930
- Pockets
- 1 · best druggability 0.55
Structure
x-ray diffraction · 2 distinct chains · 91% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleocapsid protein | protein | 74 | 91% helix, 0% strand | Q81930 |
| B | Nucleocapsid protein | protein | 71 | 92% helix, 0% strand | Q81930 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 211 | 0.55 | 0.79 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 339 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 2IC9 · The Coiled-coil Domain (residues 1-93) Structure of the Sin Nombre Virus Nucleocapsid… · 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 Q81930
- Elsewhere: RCSB PDB 2IC9 · PDBe 2IC9 · UniProt Q81930
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