Research workbench
AlphaFold monomer V2.0 prediction for endo-1,4-beta-XYLANASE/FERULOYL esterase (D5EY13)
Analyse AlphaFold monomer V2.0 prediction for endo-1,4-beta-XYLANASE/FERULOYL esterase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- D5EY13
- Type
- protein
- Length
- 726 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB9e066fD904660Ded6b995A83423620c085a3D96
- Molecule
- Endo-1,4-beta-XYLANASE/FERULOYL esterase
- UniProt
- D5EY13
- Pockets
- 5 · best druggability 0.77
Structure
1 distinct chain · 31% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endo-1,4-beta-XYLANASE/FERULOYL esterase | protein | 726 | 31% helix, 25% strand | D5EY13 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1118 | 0.77 | 0.79 | 93 | empty |
| 2 | 93 | 0.48 | 0.82 | 23 | empty |
| 3 | 71 | 0.41 | 0.80 | 16 | empty |
| 4 | 82 | 0.31 | 0.73 | 23 | empty |
| 5 | 60 | 0.31 | 0.75 | 15 | 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 D5EY13
- Elsewhere: UniProt D5EY13 · AlphaFold DB D5EY13
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