Research workbench
AlphaFold monomer V2.0 prediction for 2,3-bisphosphoglycerate- dependent phosphoglycerate mutase (Q0A915)
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
- Q0A915
- Type
- protein
- Length
- 232 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xD08fc2CFCBB59D4F39094eb15372af9cE86A61f6
- UniProt
- Q0A915
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 232 | — | Q0A915 |
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 Q0A915
- Elsewhere: UniProt Q0A915 · AlphaFold DB Q0A915
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