Research workbench
AlphaFold monomer V2.0 prediction for 2,3-bisphosphoglycerate- dependent phosphoglycerate mutase (A6L9K8)
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
- A6L9K8
- Type
- protein
- Length
- 248 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbb2F1C7CB3A1eeFAc24fCa72cc627162D5413FD7
- Molecule
- 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
- UniProt
- A6L9K8
- Pockets
- 2 · best druggability 0.77
Structure
1 distinct chain · 46% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase | protein | 248 | 46% helix, 15% strand | A6L9K8 |
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 | 110 | 0.77 | 0.97 | 23 | empty |
| 2 | 55 | 0.42 | 0.82 | 14 | 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 A6L9K8
- Elsewhere: UniProt A6L9K8 · AlphaFold DB A6L9K8
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