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AlphaFold monomer V2.0 prediction for succinate--CoA ligase [ADP- forming] subunit beta (P45101)
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
- P45101
- Type
- protein
- Length
- 389 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xc2C3F148eB26FE91165F4EE55FE4D2E3738B0950
- Molecule
- Succinate--CoA ligase [ADP-forming] subunit beta
- UniProt
- P45101
- Pockets
- 3 · best druggability 0.65
Structure
1 distinct chain · 38% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Succinate--CoA ligase [ADP-forming] subunit beta | protein | 389 | 38% helix, 25% strand | P45101 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 357 | 0.65 | 0.80 | 40 | empty |
| 2 | 60 | 0.31 | 0.75 | 15 | empty |
| 3 | 59 | 0.25 | 0.72 | 18 | 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 P45101
- Elsewhere: UniProt P45101 · AlphaFold DB P45101
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