Research workbench
AlphaFold monomer V2.0 prediction for 2,3-bisphosphoglycerate- dependent phosphoglycerate mutase (A0AKV8)
Analyse AlphaFold monomer V2.0 prediction for 2,3-bisphosphoglycerate- dependent… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A0AKV8
- Type
- protein
- Length
- 229 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7FDF8b382C6a36A8772D1A265E8e480c7DF0A9C1
- Molecule
- 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
- UniProt
- A0AKV8
- Pockets
- 1 · best druggability 0.60
Structure
1 distinct chain · 44% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase | protein | 229 | 44% helix, 14% strand | A0AKV8 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 152 | 0.60 | 0.84 | 23 | 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 A0AKV8
- Elsewhere: UniProt A0AKV8 · AlphaFold DB A0AKV8
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