Research workbench
AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase 5 (G4MLU0)
Analyse AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase 5 (G4MLU0) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- G4MLU0
- Type
- protein
- Length
- 405 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x35612D34a32C306CA4fc1edA9360D1F717e25950
- Molecule
- Endo-1,4-beta-xylanase 5
- UniProt
- G4MLU0
- Pockets
- 2 · best druggability 0.54
Structure
1 distinct chain · 36% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endo-1,4-beta-xylanase 5 | protein | 405 | 36% helix, 16% strand | G4MLU0 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 352 | 0.54 | 0.74 | 38 | empty |
| 2 | 87 | 0.37 | 0.76 | 19 | 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 G4MLU0
- Elsewhere: UniProt G4MLU0 · AlphaFold DB G4MLU0
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