Research workbench
AlphaFold monomer V2.0 prediction for aspartate carbamoyltransferase (Q2FN12)
Analyse AlphaFold monomer V2.0 prediction for aspartate carbamoyltransferase (Q2FN12) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q2FN12
- Type
- protein
- Length
- 298 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5c4adF1416281C09AE8eE1cbb80fF7e44cE86F97
- Molecule
- Aspartate carbamoyltransferase
- UniProt
- Q2FN12
- Pockets
- 1 · best druggability 0.65
Structure
1 distinct chain · 46% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aspartate carbamoyltransferase | protein | 298 | 46% helix, 16% strand | Q2FN12 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 299 | 0.65 | 0.82 | 36 | 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 Q2FN12
- Elsewhere: UniProt Q2FN12 · AlphaFold DB Q2FN12
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