Research workbench
AlphaFold monomer V2.0 prediction for bifunctional glutamine synthetase ADENYLYLTRANSFERASE/ADENYLYL-removing enzyme (A1S909)
Analyse AlphaFold monomer V2.0 prediction for bifunctional glutamine synthetase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A1S909
- Type
- protein
- Length
- 961 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBF0D2e107Ce1EcD2C4369B042274201DB719AaAF
- Molecule
- Bifunctional glutamine synthetase ADENYLYLTRANSFERASE/ADENYLYL-removing enzyme
- UniProt
- A1S909
- Pockets
- 11 · best druggability 0.66
Structure
1 distinct chain · 62% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional glutamine synthetase ADENYLYLTRANSFERASE/ADENYLYL-removing enzyme | protein | 961 | 62% helix, 7% strand | A1S909 |
Pockets
11 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 442 | 0.66 | 0.79 | 39 | empty |
| 2 | 395 | 0.65 | 0.78 | 26 | empty |
| 3 | 304 | 0.55 | 0.76 | 31 | empty |
| 4 | 62 | 0.47 | 0.84 | 11 | empty |
| 5 | 149 | 0.46 | 0.77 | 20 | empty |
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 A1S909
- Elsewhere: UniProt A1S909 · AlphaFold DB A1S909
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