Research workbench
AlphaFold monomer V2.0 prediction for peptide-N(4)-(N-acetyl-beta- GLUCOSAMINYL)ASPARAGINE amidase (Q5WNE3)
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
- Q5WNE3
- Type
- protein
- Length
- 602 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0D671490EE06E75975e90D7F99F73B20BE618744
- Molecule
- Peptide-N(4)-(N-acetyl-beta-GLUCOSAMINYL)ASPARAGINE amidase
- UniProt
- Q5WNE3
- Pockets
- 8 · best druggability 0.75
Structure
1 distinct chain · 32% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptide-N(4)-(N-acetyl-beta-GLUCOSAMINYL)ASPARAGINE amidase | protein | 602 | 32% helix, 28% strand | Q5WNE3 |
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1047 | 0.75 | 0.78 | 67 | empty |
| 2 | 301 | 0.57 | 0.77 | 38 | empty |
| 3 | 212 | 0.52 | 0.77 | 32 | empty |
| 4 | 148 | 0.45 | 0.76 | 30 | empty |
| 5 | 107 | 0.42 | 0.77 | 18 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
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 Q5WNE3
- Elsewhere: UniProt Q5WNE3 · AlphaFold DB Q5WNE3
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