Research workbench
AlphaFold monomer V2.0 prediction for 2,3-bisphosphoglycerate- dependent phosphoglycerate mutase (B2TUY6)
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
- B2TUY6
- Type
- protein
- Length
- 250 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x2286c6C31A3636A92d0a0BE4443E4A3e89CDa574
- Molecule
- 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
- UniProt
- B2TUY6
- Pockets
- 3 · best druggability 0.76
Structure
1 distinct chain · 46% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase | protein | 250 | 46% helix, 14% strand | B2TUY6 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 106 | 0.76 | 0.97 | 23 | empty |
| 2 | 56 | 0.35 | 0.78 | 13 | empty |
| 3 | 56 | 0.28 | 0.74 | 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 B2TUY6
- Elsewhere: UniProt B2TUY6 · AlphaFold DB B2TUY6
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