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AlphaFold monomer V2.0 prediction for succinate--CoA ligase [ADP- forming] subunit beta (A0LRU4)
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
- A0LRU4
- Type
- protein
- Length
- 392 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xb8D26B2A804f01ae9F25bc6F07fB7e42852BC131
- Molecule
- Succinate--CoA ligase [ADP-forming] subunit beta
- UniProt
- A0LRU4
- Pockets
- 2 · best druggability 0.66
Structure
1 distinct chain · 41% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Succinate--CoA ligase [ADP-forming] subunit beta | protein | 392 | 41% helix, 25% strand | A0LRU4 |
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 | 319 | 0.66 | 0.81 | 39 | empty |
| 2 | 138 | 0.42 | 0.75 | 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 A0LRU4
- Elsewhere: UniProt A0LRU4 · AlphaFold DB A0LRU4
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