Research workbench
AlphaFold monomer V2.0 prediction for succinate--CoA ligase [ADP- forming] subunit beta (A9L532)
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
- A9L532
- Type
- protein
- Length
- 388 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0dDe1C2158EcB65931D4C160486DEFc2f9bC7D1c
- Molecule
- Succinate--CoA ligase [ADP-forming] subunit beta
- UniProt
- A9L532
- Pockets
- 1 · best druggability 0.64
Structure
1 distinct chain · 39% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Succinate--CoA ligase [ADP-forming] subunit beta | protein | 388 | 39% helix, 26% strand | A9L532 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 330 | 0.64 | 0.80 | 43 | 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 A9L532
- Elsewhere: UniProt A9L532 · AlphaFold DB A9L532
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