Research workbench
Crystallographic analysis of rotavirus NSP2-RNA complex reveals specific recognition of 5'-gg sequence for rtpase activity
Analyse Crystallographic analysis of rotavirus NSP2-RNA complex reveals specific… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4G0J
- Type
- protein
- Length
- 2,900 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Non-structural protein 2
- EC
- 3.6.4.-
- UniProt
- Q03243
- Pockets
- 20 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J | Non-structural protein 2 (EC 3.6.4.-) | protein | 290 | 41% helix, 15% strand | Q03243 |
Pockets
20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1096 | 0.79 | 0.81 | 98 | empty |
| 2 | 583 | 0.79 | 0.85 | 45 | empty |
| 3 | 1123 | 0.78 | 0.80 | 110 | empty |
| 4 | 987 | 0.76 | 0.78 | 90 | empty |
| 5 | 1023 | 0.74 | 0.77 | 75 | empty |
Interfaces
10 interfaces between chains.
- A–G · 772 Ų buried · 23 hydrogen bonds · protein-protein
- D–E · 704 Ų buried · 7 hydrogen bonds · protein-protein
- H–I · 702 Ų buried · 4 hydrogen bonds · protein-protein
- C–J · 387 Ų buried · 9 hydrogen bonds · protein-protein
- B–J · 235 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 4G0J · Crystallographic Analysis of Rotavirus NSP2-RNA Complex Reveals Specific Recognition of… · 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 Q03243
- Elsewhere: RCSB PDB 4G0J · PDBe 4G0J · UniProt Q03243
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