Research workbench
AlphaFold monomer V2.0 prediction for glucose-1-phosphate adenylyltransferase (P39122)
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
- P39122
- Type
- protein
- Length
- 380 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB35df660264f41795De49C83276C108A4ba91ADE
- Molecule
- Glucose-1-phosphate adenylyltransferase
- UniProt
- P39122
- Pockets
- 3 · best druggability 0.70
Structure
1 distinct chain · 26% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glucose-1-phosphate adenylyltransferase | protein | 380 | 26% helix, 28% strand | P39122 |
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 | 443 | 0.70 | 0.81 | 38 | empty |
| 2 | 97 | 0.36 | 0.75 | 21 | empty |
| 3 | 69 | 0.30 | 0.74 | 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 P39122
- Elsewhere: UniProt P39122 · AlphaFold DB P39122
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