MolNFT v1 · #440774 · protein
AlphaFold monomer V2.0 prediction for succinate--CoA ligase [ADP- forming] subunit beta (Q5HC25)
Q5HC25 · Succinate--CoA ligase [ADP-forming] subunit beta: “AlphaFold monomer V2.0 prediction for succinate--CoA ligase [ADP- forming] subunit beta (Q5HC25)”. 2 pockets (best druggability 0.63). MolNFT v1 #440774 on GenesisL1: 3D…
- Accession
- Q5HC25
- Type
- protein
- Length
- 386 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9B130d619fCFc21d0D08E5Ce38Cf42A5fbe230CB
- Molecule
- Succinate--CoA ligase [ADP-forming] subunit beta
- UniProt
- Q5HC25
- Pockets
- 2 · best druggability 0.63
Structure
1 distinct chain · 40% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Succinate--CoA ligase [ADP-forming] subunit beta | protein | 386 | 40% helix, 25% strand | Q5HC25 |
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 | 333 | 0.63 | 0.79 | 40 | empty |
| 2 | 126 | 0.36 | 0.73 | 25 | 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 Q5HC25
- Elsewhere: UniProt Q5HC25 · AlphaFold DB Q5HC25
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