Research workbench
AlphaFold monomer V2.0 prediction for succinate--CoA ligase [ADP- forming] subunit beta (B8GCC9)
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
- B8GCC9
- Type
- protein
- Length
- 382 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x80D2ac0F5e3268bC5C1d28BBAA07E3169BB02b79
- Molecule
- Succinate--CoA ligase [ADP-forming] subunit beta
- UniProt
- B8GCC9
- Pockets
- 3 · 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 | 382 | 40% helix, 26% strand | B8GCC9 |
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 | 331 | 0.62 | 0.79 | 42 | empty |
| 2 | 117 | 0.38 | 0.74 | 19 | empty |
| 3 | 55 | 0.32 | 0.77 | 13 | 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 B8GCC9
- Elsewhere: UniProt B8GCC9 · AlphaFold DB B8GCC9
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