Research workbench
AlphaFold monomer V2.0 prediction for peptide-N(4)-(N-acetyl-beta- GLUCOSAMINYL)ASPARAGINE amidase (Q6CAX5)
Analyse AlphaFold monomer V2.0 prediction for peptide-N(4)-(N-acetyl-beta… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q6CAX5
- Type
- protein
- Length
- 356 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x1Ce155A2258661A2eA50795DE5b0318ee956a5A1
- Molecule
- Peptide-N(4)-(N-acetyl-beta-GLUCOSAMINYL)ASPARAGINE amidase
- UniProt
- Q6CAX5
- Pockets
- 4 · best druggability 0.61
Structure
1 distinct chain · 48% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptide-N(4)-(N-acetyl-beta-GLUCOSAMINYL)ASPARAGINE amidase | protein | 356 | 48% helix, 15% strand | Q6CAX5 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 277 | 0.61 | 0.80 | 40 | empty |
| 2 | 177 | 0.46 | 0.76 | 23 | empty |
| 3 | 198 | 0.45 | 0.74 | 30 | empty |
| 4 | 72 | 0.31 | 0.75 | 18 | 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 Q6CAX5
- Elsewhere: UniProt Q6CAX5 · AlphaFold DB Q6CAX5
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