Research workbench
AlphaFold monomer V2.0 prediction for succinate--CoA ligase [ADP- forming] subunit beta (Q2FHJ3)
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
- Q2FHJ3
- Type
- protein
- Length
- 388 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xD28dBF051Fa42188710bD32965c7B1a5507E41f2
- Molecule
- Succinate--CoA ligase [ADP-forming] subunit beta
- UniProt
- Q2FHJ3
- Pockets
- 2 · best druggability 0.66
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 | Q2FHJ3 |
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 | 312 | 0.66 | 0.81 | 38 | empty |
| 2 | 90 | 0.34 | 0.74 | 14 | 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 Q2FHJ3
- Elsewhere: UniProt Q2FHJ3 · AlphaFold DB Q2FHJ3
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.