Research workbench
Nodamura virus protein B2, RNA-binding domain
Analyse Nodamura virus protein B2, RNA-binding domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3G80
- Type
- protein
- Length
- 146 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein B2
- UniProt
- Q9IMM3
Structure
x-ray diffraction · 2 distinct chains · 81% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein B2 | protein | 73 | 81% helix, 0% strand | Q9IMM3 |
| B | Protein B2 | protein | 73 | 81% helix, 0% strand | Q9IMM3 |
Interfaces
1 interface between chains.
- A–B · 1399 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 3G80 · Nodamura virus protein b2, RNA-binding domain · 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 Q9IMM3
- Elsewhere: RCSB PDB 3G80 · PDBe 3G80 · UniProt Q9IMM3
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