Research workbench
Dimeric structure of D347G D348G mutant of the sapporovirus RNA dependent RNA polymerase
Analyse Dimeric structure of D347G D348G mutant of the sapporovirus RNA dependent RNA… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WK4
- Type
- protein
- Length
- 1,001 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.98
- Source
- SAPPORO VIRUS
- Molecule
- Protease-polymerase P70
- EC
- 3.4.22.66
- UniProt
- Q69014
- Pockets
- 9 · best druggability 0.72
Structure
x-ray diffraction · resolution 2.98 · 2 distinct chains · 43% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protease-polymerase P70 (EC 3.4.22.66) | protein | 499 | 43% helix, 16% strand | Q69014 |
| B | Protease-polymerase P70 (EC 3.4.22.66) | protein | 502 | 43% helix, 15% strand | Q69014 |
Ligands and binding sites
- GOL · Glycerol · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 950 | 0.72 | 0.76 | 71 | empty |
| 2 | 888 | 0.71 | 0.76 | 75 | empty |
| 3 | 55 | 0.70 | 0.98 | 19 | empty |
| 4 | 602 | 0.69 | 0.78 | 71 | GOL |
| 5 | 423 | 0.60 | 0.76 | 47 | empty |
Interfaces
1 interface between chains.
- A–B · 1635 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 2WK4 · Dimeric structure of D347G D348G mutant of the sapporovirus RNA dependent RNA polymerase · 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 Q69014
- Elsewhere: RCSB PDB 2WK4 · PDBe 2WK4 · UniProt Q69014
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