Research workbench
AlphaFold monomer V2.0 prediction for peptide-N(4)-(N-acetyl-beta- GLUCOSAMINYL)ASPARAGINE amidase (Q75D29)
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
- Q75D29
- Type
- protein
- Length
- 350 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xF3ACd2a4D8BeEE52Ec7E86d2C7c482Bf354b139B
- Molecule
- Peptide-N(4)-(N-acetyl-beta-GLUCOSAMINYL)ASPARAGINE amidase
- UniProt
- Q75D29
- Pockets
- 2 · best druggability 0.65
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 | 350 | 48% helix, 15% strand | Q75D29 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 404 | 0.65 | 0.79 | 39 | empty |
| 2 | 265 | 0.53 | 0.76 | 39 | 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 Q75D29
- Elsewhere: UniProt Q75D29 · AlphaFold DB Q75D29
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