Research workbench
AlphaFold monomer V2.0 prediction for 2,3-bisphosphoglycerate- independent phosphoglycerate mutase (A5WA89)
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
- A5WA89
- Type
- protein
- Length
- 511 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xEa58c7534E5701aA8370E0fAEb19b7e14653e69c
- Molecule
- 2,3-bisphosphoglycerate-independent phosphoglycerate mutase
- UniProt
- A5WA89
- Pockets
- 3 · best druggability 0.50
Structure
1 distinct chain · 38% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 2,3-bisphosphoglycerate-independent phosphoglycerate mutase | protein | 511 | 38% helix, 18% strand | A5WA89 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 272 | 0.50 | 0.74 | 35 | empty |
| 2 | 67 | 0.34 | 0.76 | 19 | empty |
| 3 | 55 | 0.30 | 0.76 | 17 | 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 A5WA89
- Elsewhere: UniProt A5WA89 · AlphaFold DB A5WA89
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