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Crystal structure of arginine kinase (AK3) from the ciliate Paramecium tetraurelia
Analyse Crystal structure of arginine kinase (AK3) from the ciliate Paramecium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7EWS
- Type
- protein
- Length
- 756 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2
- Source
- Paramecium tetraurelia
- Molecule
- arginine kinase
- UniProt
- A0C7I4
- Pockets
- 8 · best druggability 0.74
Structure
x-ray diffraction · resolution 2 · 1 distinct chain · 41% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | arginine kinase | protein | 378 | 41% helix, 17% strand | A0C7I4 |
Pockets
8 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 685 | 0.74 | 0.80 | 55 | empty |
| 2 | 252 | 0.69 | 0.85 | 32 | empty |
| 3 | 447 | 0.69 | 0.81 | 38 | empty |
| 4 | 289 | 0.64 | 0.81 | 25 | empty |
| 5 | 142 | 0.53 | 0.80 | 32 | empty |
Interfaces
1 interface between chains.
- A–B · 1028 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 7EWS · Crystal structure of arginine kinase (AK3) from the ciliate paramecium tetraurelia · 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 A0C7I4
- Elsewhere: RCSB PDB 7EWS · PDBe 7EWS · UniProt A0C7I4
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