Research workbench
AlphaFold monomer V2.0 prediction for succinate--CoA ligase [ADP- forming] subunit beta (Q021N6)
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
- Q021N6
- Type
- protein
- Length
- 384 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x71112d4fF7ebb3b617963c05f052289e073082FD
- Molecule
- Succinate--CoA ligase [ADP-forming] subunit beta
- UniProt
- Q021N6
- Pockets
- 2 · best druggability 0.62
Structure
1 distinct chain · 40% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Succinate--CoA ligase [ADP-forming] subunit beta | protein | 384 | 40% helix, 26% strand | Q021N6 |
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 | 303 | 0.62 | 0.79 | 37 | empty |
| 2 | 167 | 0.41 | 0.73 | 27 | 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 Q021N6
- Elsewhere: UniProt Q021N6 · AlphaFold DB Q021N6
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