Research workbench
AlphaFold monomer V2.0 prediction for 2,3-bisphosphoglycerate- independent phosphoglycerate mutase (A9N970)
Analyse AlphaFold monomer V2.0 prediction for 2,3-bisphosphoglycerate- independent… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A9N970
- Type
- protein
- Length
- 519 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf868de599Ee83DBA5E1A993E4C2FC610ac38Bcff
- Molecule
- 2,3-bisphosphoglycerate-independent phosphoglycerate mutase
- UniProt
- A9N970
- Pockets
- 2 · best druggability 0.68
Structure
1 distinct chain · 38% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 2,3-bisphosphoglycerate-independent phosphoglycerate mutase | protein | 519 | 38% helix, 18% strand | A9N970 |
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 | 508 | 0.68 | 0.78 | 42 | empty |
| 2 | 90 | 0.39 | 0.77 | 16 | 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 A9N970
- Elsewhere: UniProt A9N970 · AlphaFold DB A9N970
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