Research workbench
Crystal structure of Terrestrivirus inositol pyrophosphate kinase in complex with ADP
Analyse Crystal structure of Terrestrivirus inositol pyrophosphate kinase in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 8T8V
- Type
- protein
- Length
- 216 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.96
- Source
- Terrestrivirus sp.
- Molecule
- Kinase
- UniProt
- A0A3G4ZNY6
- Ligands
- ADP, MG, PO4
- Pockets
- 2 · best druggability 0.74
Structure
x-ray diffraction · resolution 1.96 · 1 distinct chain · 37% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Kinase | protein | 216 | 37% helix, 23% strand | A0A3G4ZNY6 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- MG · Magnesium ion · metal · 2 copies · chains A
- PO4 · Phosphate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 418 | 0.74 | 0.84 | 47 | ADP, MG, PO4 |
| 2 | 100 | 0.38 | 0.75 | 16 | empty |
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 A0A3G4ZNY6
- Elsewhere: RCSB PDB 8T8V · PDBe 8T8V · UniProt A0A3G4ZNY6
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