Research workbench
AlphaFold monomer V2.0 prediction for bifunctional endo-1,4-beta- xylanase xyla (P29126)
Analyse AlphaFold monomer V2.0 prediction for bifunctional endo-1,4-beta- xylanase xyla… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P29126
- Type
- protein
- Length
- 954 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xD078c9CbF2729549ADF337b0f5AB69B760a74D2e
- Molecule
- Bifunctional endo-1,4-beta-xylanase xyla
- UniProt
- P29126
- Pockets
- 6 · best druggability 0.75
Structure
1 distinct chain · 18% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional endo-1,4-beta-xylanase xyla | protein | 954 | 18% helix, 31% strand | P29126 |
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 609 | 0.75 | 0.82 | 67 | empty |
| 2 | 581 | 0.66 | 0.76 | 54 | empty |
| 3 | 273 | 0.60 | 0.79 | 33 | empty |
| 4 | 78 | 0.32 | 0.74 | 16 | empty |
| 5 | 56 | 0.29 | 0.75 | 18 | 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 P29126
- Elsewhere: UniProt P29126 · AlphaFold DB P29126
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