MolNFT v1 · #502509 · protein
AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase B (P26223)
P26223: “AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase B (P26223)”. 4 pockets (best druggability 0.62). MolNFT v1 #502509 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- P26223
- Type
- protein
- Length
- 635 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7f973A429380a62660524FB40bC00A4B9D9D48a2
- Molecule
- Endo-1,4-beta-xylanase B
- UniProt
- P26223
- Pockets
- 4 · best druggability 0.62
Structure
1 distinct chain · 40% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endo-1,4-beta-xylanase B | protein | 635 | 40% helix, 18% strand | P26223 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 576 | 0.62 | 0.74 | 49 | empty |
| 2 | 234 | 0.54 | 0.77 | 33 | empty |
| 3 | 72 | 0.34 | 0.75 | 17 | empty |
| 4 | 55 | 0.27 | 0.74 | 13 | 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 P26223
- Elsewhere: UniProt P26223 · AlphaFold DB P26223
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