Research workbench
AlphaFold monomer V2.0 prediction for peptide-N(4)-(N-acetyl-beta- GLUCOSAMINYL)ASPARAGINE amidase (Q02890)
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
- Q02890
- Type
- protein
- Length
- 363 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7FDF8b382C6a36A8772D1A265E8e480c7DF0A9C1
- Molecule
- Peptide-N(4)-(N-acetyl-beta-GLUCOSAMINYL)ASPARAGINE amidase
- UniProt
- Q02890
- Pockets
- 6 · best druggability 0.64
Structure
1 distinct chain · 48% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptide-N(4)-(N-acetyl-beta-GLUCOSAMINYL)ASPARAGINE amidase | protein | 363 | 48% helix, 17% strand | Q02890 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 334 | 0.64 | 0.80 | 34 | empty |
| 2 | 169 | 0.59 | 0.82 | 23 | empty |
| 3 | 181 | 0.46 | 0.75 | 25 | empty |
| 4 | 103 | 0.43 | 0.78 | 16 | empty |
| 5 | 112 | 0.36 | 0.74 | 23 | empty |
Compared structures
- 3ESW · Complex of yeast PNGase with GlcNAc2-IAc. · an experimental structure of the same protein · chain A against A, TM-score 0.89
- 3ESW · Complex of yeast pngase with GLCNAC2-iac. · an experimental structure of the same protein · chain A against A, TM-score 0.89
- 1X3W · Structure of a peptide:N-glycanase-Rad23 complex · an experimental structure of the same protein · chain A against A, TM-score 0.87
- 1X3W · Structure of a PEPTIDE:N-glycanase-RAD23 complex · an experimental structure of the same protein · chain A against A, TM-score 0.87
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 Q02890
- Elsewhere: UniProt Q02890 · AlphaFold DB Q02890
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