Research workbench
The structure of a CoA pyrophosphatase from D. Radiodurans
Analyse The structure of a CoA pyrophosphatase from D. Radiodurans in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1NQY
- Type
- protein
- Length
- 170 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.09
- Source
- Deinococcus radiodurans
- Molecule
- CoA pyrophosphatase (MutT/nudix family protein)
- EC
- 3.6.1.9
- UniProt
- Q9RV46
- Pockets
- 1 · best druggability 0.56
Structure
x-ray diffraction · resolution 2.09 · 1 distinct chain · 25% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CoA pyrophosphatase (MutT/nudix family protein) (EC 3.6.1.9) | protein | 170 | 25% helix, 38% strand | Q9RV46 |
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 | 52 | 0.56 | 0.91 | 17 | empty |
Compared structures
- 1NQY · The structure of a CoA pyrophosphatase from D. radiodurans · 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 Q9RV46
- Elsewhere: RCSB PDB 1NQY · PDBe 1NQY · UniProt Q9RV46
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