Research workbench
AlphaFold monomer V2.0 prediction for probable xyloglucan ENDOTRANSGLUCOSYLASE/HYDROLASE protein 12 (Q9FKL9)
Analyse AlphaFold monomer V2.0 prediction for probable xyloglucan… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9FKL9
- Type
- protein
- Length
- 285 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7c75F0f7d6d136A2b8D4C6C6e9b3D8a697949DF1
- Molecule
- Probable xyloglucan ENDOTRANSGLUCOSYLASE/HYDROLASE protein 12
- UniProt
- Q9FKL9
- Pockets
- 1 · best druggability 0.34
Structure
1 distinct chain · 13% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable xyloglucan ENDOTRANSGLUCOSYLASE/HYDROLASE protein 12 | protein | 285 | 13% helix, 38% strand | Q9FKL9 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 61 | 0.34 | 0.77 | 18 | empty |
Modifications
Observed in the structure: 2 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 Q9FKL9
- Elsewhere: UniProt Q9FKL9 · AlphaFold DB Q9FKL9
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