Research workbench
AlphaFold monomer V2.0 prediction for bifunctional glutamine synthetase ADENYLYLTRANSFERASE/ADENYLYL-removing enzyme (Q1CMD5)
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
- Q1CMD5
- Type
- protein
- Length
- 951 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x1ad771C934EF56ebFF74f7581CB73023aCA831d3
- Molecule
- Bifunctional glutamine synthetase ADENYLYLTRANSFERASE/ADENYLYL-removing enzyme
- UniProt
- Q1CMD5
- Pockets
- 16 · best druggability 0.63
Structure
1 distinct chain · 63% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional glutamine synthetase ADENYLYLTRANSFERASE/ADENYLYL-removing enzyme | protein | 951 | 63% helix, 7% strand | Q1CMD5 |
Pockets
16 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 380 | 0.63 | 0.78 | 34 | empty |
| 2 | 315 | 0.59 | 0.77 | 25 | empty |
| 3 | 83 | 0.56 | 0.86 | 14 | empty |
| 4 | 275 | 0.50 | 0.73 | 40 | empty |
| 5 | 174 | 0.49 | 0.77 | 22 | 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 Q1CMD5
- Elsewhere: UniProt Q1CMD5 · AlphaFold DB Q1CMD5
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