Research workbench
AlphaFold monomer V2.0 prediction for succinate--CoA ligase [ADP- forming] subunit beta (B1YVY6)
Analyse AlphaFold monomer V2.0 prediction for succinate--CoA ligase [ADP- forming]… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B1YVY6
- Type
- protein
- Length
- 388 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x01e98F6aA2b8835b76ABa5D63df70C33997ED954
- Molecule
- Succinate--CoA ligase [ADP-forming] subunit beta
- UniProt
- B1YVY6
- Pockets
- 2 · best druggability 0.65
Structure
1 distinct chain · 39% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Succinate--CoA ligase [ADP-forming] subunit beta | protein | 388 | 39% helix, 25% strand | B1YVY6 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 334 | 0.65 | 0.80 | 48 | empty |
| 2 | 110 | 0.35 | 0.73 | 26 | 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 B1YVY6
- Elsewhere: UniProt B1YVY6 · AlphaFold DB B1YVY6
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.