Research workbench
AlphaFold monomer V2.0 prediction for glucosamine 6-phosphate N-acetyltransferase (Q17427)
Analyse AlphaFold monomer V2.0 prediction for glucosamine 6-phosphate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q17427
- Type
- protein
- Length
- 165 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xb4D2d9c96b0D792d0b77e7147D724cc1F801ae58
- UniProt
- Q17427
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 165 | — | Q17427 |
Compared structures
- 4AG9 · C. elegans glucosamine-6-phosphate N-acetyltransferase (GNA1): ternary complex with… · an experimental structure of the same protein · chain A against A, TM-score 0.98
- 4AG9 · C. elegans glucosamine-6-phosphate N-acetyltransferase (GNA1): ternary complex with… · an experimental structure of the same protein · chain A against A, TM-score 0.98
- 4AG7 · C. elegans glucosamine-6-phosphate N-acetyltransferase (GNA1): coenzyme A adduct · an experimental structure of the same protein · chain A against B, TM-score 0.96
- 4AG7 · C. elegans glucosamine-6-phosphate N-acetyltransferase (GNA1): coenzyme a adduct · an experimental structure of the same protein · chain A against B, TM-score 0.96
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 Q17427
- Elsewhere: UniProt Q17427 · AlphaFold DB Q17427
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