Research workbench
AlphaFold monomer V2.0 prediction for 2,3-bisphosphoglycerate- dependent phosphoglycerate mutase (Q64R85)
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
- Q64R85
- Type
- protein
- Length
- 248 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5c4adF1416281C09AE8eE1cbb80fF7e44cE86F97
- UniProt
- Q64R85
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 248 | — | Q64R85 |
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 Q64R85
- Elsewhere: UniProt Q64R85 · AlphaFold DB Q64R85
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