Research workbench
ADP ribose pyrophosphatase from thermus thermophilus HB8 in apo state at 0.92 ångström resolution
Analyse ADP ribose pyrophosphatase from thermus thermophilus HB8 in apo state at 0.92… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3X0J
- Type
- protein
- Length
- 157 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ADP-ribose pyrophosphatase
- EC
- 3.6.1.13
- UniProt
- Q84CU3
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.45
Structure
x-ray diffraction · 1 distinct chain · 22% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ADP-ribose pyrophosphatase (EC 3.6.1.13) | protein | 157 | 22% helix, 45% strand | Q84CU3 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 179 | 0.45 | 0.74 | 23 | GOL, SO4 |
Compared structures
- 3X0J · ADP ribose pyrophosphatase from Thermus thermophilus HB8 in apo state at 0.92 angstrom… · 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 Q84CU3
- Elsewhere: RCSB PDB 3X0J · PDBe 3X0J · UniProt Q84CU3
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