Research workbench
AlphaFold monomer V2.0 prediction for phosphoglucosamine mutase (B1XP15)
Analyse AlphaFold monomer V2.0 prediction for phosphoglucosamine mutase (B1XP15) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B1XP15
- Type
- protein
- Length
- 481 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x29EAdEfF44bDA42f96B33481D606dd403a9e4547
- UniProt
- B1XP15
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 481 | — | B1XP15 |
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 B1XP15
- Elsewhere: UniProt B1XP15 · AlphaFold DB B1XP15
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