Research workbench
AlphaFold monomer V2.0 prediction for peptide-N(4)-(N-acetyl-beta- GLUCOSAMINYL)ASPARAGINE amidase (Q503I8)
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
- Q503I8
- Type
- protein
- Length
- 644 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xc6d218717d301db99821336bD1A653378bD07abd
- Molecule
- Peptide-N(4)-(N-acetyl-beta-GLUCOSAMINYL)ASPARAGINE amidase
- UniProt
- Q503I8
- Pockets
- 4 · best druggability 0.69
Structure
1 distinct chain · 37% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptide-N(4)-(N-acetyl-beta-GLUCOSAMINYL)ASPARAGINE amidase | protein | 644 | 37% helix, 24% strand | Q503I8 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 823 | 0.69 | 0.76 | 67 | empty |
| 2 | 701 | 0.67 | 0.75 | 65 | empty |
| 3 | 140 | 0.49 | 0.78 | 21 | empty |
| 4 | 88 | 0.32 | 0.73 | 17 | 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 Q503I8
- Elsewhere: UniProt Q503I8 · AlphaFold DB Q503I8
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