Research workbench
AlphaFold monomer V2.0 prediction for phosphoglucosamine mutase (O34824)
Analyse AlphaFold monomer V2.0 prediction for phosphoglucosamine mutase (O34824) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- O34824
- Type
- protein
- Length
- 448 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf23FAc8E9E29c5e2e2c0614b611FB353464fD274
- UniProt
- O34824
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 448 | — | O34824 |
Compared structures
- 7OML · Bacillus subtilis phosphoglucomutase glmm (metal bound) · an experimental structure of the same protein · chain A against A, TM-score 0.93
- 7OJR · Bacillus subtilis phosphoglucomutase glmm (phosphate bound) · an experimental structure of the same protein · chain A against A, TM-score 0.93
- 7OLH · Bacillus subtilis complex structure 1 of diadenylate cyclase cdaa cytoplasmic domain… · an experimental structure of the same protein · chain A against A, TM-score 0.82
- 7OLH · Bacillus subtilis Complex structure 1 of diadenylate cyclase CdaA cytoplasmic domain… · an experimental structure of the same protein · chain A against A, TM-score 0.82
- 7OJS · Complex structure 2 of the bacillus subtilis cdaa C-di-AMP cyclase domain (cdaacd) and… · an experimental structure of the same protein · chain A against C, TM-score 0.81
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 O34824
- Elsewhere: UniProt O34824 · AlphaFold DB O34824
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