Research workbench
AlphaFold monomer V2.0 prediction for glucose-1-phosphate adenylyltransferase (C0MH79)
Analyse AlphaFold monomer V2.0 prediction for glucose-1-phosphate adenylyltransferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- C0MH79
- Type
- protein
- Length
- 379 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5c4adF1416281C09AE8eE1cbb80fF7e44cE86F97
- Molecule
- Glucose-1-phosphate adenylyltransferase
- UniProt
- C0MH79
- Pockets
- 3 · best druggability 0.65
Structure
1 distinct chain · 25% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glucose-1-phosphate adenylyltransferase | protein | 379 | 25% helix, 29% strand | C0MH79 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 426 | 0.65 | 0.78 | 44 | empty |
| 2 | 96 | 0.40 | 0.76 | 23 | empty |
| 3 | 84 | 0.34 | 0.75 | 16 | 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 C0MH79
- Elsewhere: UniProt C0MH79 · AlphaFold DB C0MH79
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