Research workbench
AlphaFold monomer V2.0 prediction for xyloglucan-specific endo- beta-1,4-glucanase a (O94218)
Analyse AlphaFold monomer V2.0 prediction for xyloglucan-specific endo… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- O94218
- Type
- protein
- Length
- 238 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xb4D2d9c96b0D792d0b77e7147D724cc1F801ae58
- Molecule
- Xyloglucan-specific endo-beta-1,4-glucanase a
- UniProt
- O94218
- Pockets
- 1 · best druggability 0.33
Structure
1 distinct chain · 7% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Xyloglucan-specific endo-beta-1,4-glucanase a | protein | 238 | 7% helix, 53% strand | O94218 |
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 | 80 | 0.33 | 0.74 | 21 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 3VL9 · Crystal structure of xeg-xyloglucan · an experimental structure of the same protein · chain A against A, TM-score 0.93
- 3VL9 · Crystal structure of xeg-xyloglucan · an experimental structure of the same protein · chain A against A, TM-score 0.93
- 3VL8 · Crystal structure of XEG · an experimental structure of the same protein · chain A against A, TM-score 0.91
- 3VL8 · Crystal structure of xeg · an experimental structure of the same protein · chain A against A, TM-score 0.91
- 3VLB · Crystal structure of xeg-edgp · an experimental structure of the same protein · chain A against B, TM-score 0.91
- 3VLB · Crystal structure of xeg-edgp · an experimental structure of the same protein · chain A against B, TM-score 0.91
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 O94218
- Elsewhere: UniProt O94218 · AlphaFold DB O94218
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