Research workbench
AlphaFold monomer V2.0 prediction for wall-associated proteinase (E9D2Q2)
Analyse AlphaFold monomer V2.0 prediction for wall-associated proteinase (E9D2Q2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- E9D2Q2
- Type
- protein
- Length
- 309 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x404dD93cd2E0F7C9B647A7c82A4C1aCbcc756C0A
- Molecule
- Wall-associated proteinase
- UniProt
- E9D2Q2
- Pockets
- 4 · best druggability 0.76
Structure
1 distinct chain · 2% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Wall-associated proteinase | protein | 309 | 2% helix, 48% strand | E9D2Q2 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 461 | 0.76 | 0.84 | 42 | empty |
| 2 | 102 | 0.49 | 0.81 | 22 | empty |
| 3 | 91 | 0.40 | 0.77 | 28 | empty |
| 4 | 84 | 0.34 | 0.74 | 19 | 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 E9D2Q2
- Elsewhere: UniProt E9D2Q2 · AlphaFold DB E9D2Q2
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