Research workbench
AlphaFold monomer V2.0 prediction for 2,3-bisphosphoglycerate- independent phosphoglycerate mutase (P51379)
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
- P51379
- Type
- protein
- Length
- 534 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3E987Aa5e233CDa0b5218C798Bb0c3527b9D4A2d
- UniProt
- P51379
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 534 | — | P51379 |
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 P51379
- Elsewhere: UniProt P51379 · AlphaFold DB P51379
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