Research workbench
AlphaFold monomer V2.0 prediction for 2,3-bisphosphoglycerate- independent phosphoglycerate mutase (Q15PS5)
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
- Q15PS5
- Type
- protein
- Length
- 511 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x85Ec3C1FF5d3d85A55436712085fA9111c2877a0
- Molecule
- 2,3-bisphosphoglycerate-independent phosphoglycerate mutase
- UniProt
- Q15PS5
- Pockets
- 2 · best druggability 0.55
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 | Q15PS5 |
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 | 388 | 0.55 | 0.74 | 42 | empty |
| 2 | 127 | 0.44 | 0.77 | 19 | 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 Q15PS5
- Elsewhere: UniProt Q15PS5 · AlphaFold DB Q15PS5
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