Research workbench
AlphaFold monomer V2.0 prediction for inactive N-acetylated-alpha- linked acidic dipeptidase-like protein 2 (Q58DX5)
Analyse AlphaFold monomer V2.0 prediction for inactive N-acetylated-alpha- linked… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q58DX5
- Type
- protein
- Length
- 795 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7c75F0f7d6d136A2b8D4C6C6e9b3D8a697949DF1
- Molecule
- Inactive N-acetylated-alpha-linked acidic dipeptidase-like protein 2
- UniProt
- Q58DX5
- Pockets
- 12 · best druggability 0.81
Structure
1 distinct chain · 38% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Inactive N-acetylated-alpha-linked acidic dipeptidase-like protein 2 | protein | 795 | 38% helix, 15% strand | Q58DX5 |
Pockets
12 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 589 | 0.81 | 0.87 | 47 | empty |
| 2 | 476 | 0.75 | 0.84 | 60 | empty |
| 3 | 89 | 0.67 | 0.92 | 19 | empty |
| 4 | 192 | 0.52 | 0.78 | 27 | empty |
| 5 | 53 | 0.51 | 0.87 | 16 | empty |
Modifications
Observed in the structure: 3 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 Q58DX5
- Elsewhere: UniProt Q58DX5 · AlphaFold DB Q58DX5
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