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AlphaFold monomer V2.0 prediction for succinate--CoA ligase [ADP- forming] subunit beta (B9IVC5)
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
- B9IVC5
- Type
- protein
- Length
- 386 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xF4089482c9F305083AE4073ef683C745B0f8C6F5
- Molecule
- Succinate--CoA ligase [ADP-forming] subunit beta
- UniProt
- B9IVC5
- Pockets
- 2 · best druggability 0.63
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 | 386 | 39% helix, 25% strand | B9IVC5 |
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 | 329 | 0.63 | 0.79 | 40 | empty |
| 2 | 78 | 0.30 | 0.73 | 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 B9IVC5
- Elsewhere: UniProt B9IVC5 · AlphaFold DB B9IVC5
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