Research workbench
AlphaFold monomer V2.0 prediction for sulfate adenylyltransferase (B2J5M3)
Analyse AlphaFold monomer V2.0 prediction for sulfate adenylyltransferase (B2J5M3) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B2J5M3
- Type
- protein
- Length
- 392 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbDA05C32aD6eE153C8C5A78dfa48d7Ba25694fea
- Molecule
- Sulfate adenylyltransferase
- UniProt
- B2J5M3
- Pockets
- 3 · best druggability 0.78
Structure
1 distinct chain · 35% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sulfate adenylyltransferase | protein | 392 | 35% helix, 17% strand | B2J5M3 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 474 | 0.78 | 0.85 | 50 | empty |
| 2 | 265 | 0.53 | 0.76 | 34 | empty |
| 3 | 69 | 0.34 | 0.76 | 13 | 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 B2J5M3
- Elsewhere: UniProt B2J5M3 · AlphaFold DB B2J5M3
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