Research workbench
AlphaFold monomer V2.0 prediction for adenylate kinase (A4SEQ7)
Analyse AlphaFold monomer V2.0 prediction for adenylate kinase (A4SEQ7) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A4SEQ7
- Type
- protein
- Length
- 218 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9F605311B7e26e76340423EfAfbE5e2EFc7A0b7C
- Molecule
- Adenylate kinase
- UniProt
- A4SEQ7
- Pockets
- 4 · best druggability 0.83
Structure
1 distinct chain · 49% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adenylate kinase | protein | 218 | 49% helix, 16% strand | A4SEQ7 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 302 | 0.83 | 0.94 | 51 | empty |
| 2 | 122 | 0.49 | 0.80 | 18 | empty |
| 3 | 63 | 0.35 | 0.77 | 13 | empty |
| 4 | 67 | 0.27 | 0.73 | 18 | 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 A4SEQ7
- Elsewhere: UniProt A4SEQ7 · AlphaFold DB A4SEQ7
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