Research workbench
Crystal Structure of Arginine Kinase wild type from Daphnia magna
Analyse Crystal Structure of Arginine Kinase wild type from Daphnia magna in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6KY2
- Type
- protein
- Length
- 359 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.87
- Source
- Daphnia magna
- Molecule
- Arginine kinase
- UniProt
- A0A0A7CK57
- Ligands
- PO4
- Pockets
- 2 · best druggability 0.34
Structure
x-ray diffraction · resolution 1.87 · 1 distinct chain · 39% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arginine kinase | protein | 359 | 39% helix, 17% strand | A0A0A7CK57 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 99 | 0.34 | 0.74 | 19 | empty |
| 2 | 91 | 0.31 | 0.72 | 16 | empty |
Compared structures
- 6KY2 · Crystal structure of arginine kinase wild type from daphnia magna · 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 A0A0A7CK57
- Elsewhere: RCSB PDB 6KY2 · PDBe 6KY2 · UniProt A0A0A7CK57
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