Research workbench
AlphaFold monomer V2.0 prediction for acetyl-coenzyme a carboxylase carboxyl transferase subunit alpha (O19903)
Analyse AlphaFold monomer V2.0 prediction for acetyl-coenzyme a carboxylase carboxyl… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- O19903
- Type
- protein
- Length
- 324 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5BeA89782341f98147F2D811B063F91F0aE7D7bF
- Molecule
- Acetyl-coenzyme a carboxylase carboxyl transferase subunit alpha
- UniProt
- O19903
- Pockets
- 2 · best druggability 0.42
Structure
1 distinct chain · 53% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetyl-coenzyme a carboxylase carboxyl transferase subunit alpha | protein | 324 | 53% helix, 15% strand | O19903 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 117 | 0.42 | 0.76 | 19 | empty |
| 2 | 77 | 0.37 | 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 O19903
- Elsewhere: UniProt O19903 · AlphaFold DB O19903
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