MolNFT v1 · #502409 · protein
AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase 1 (P36218)
P36218: “AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase 1 (P36218)”. 1 pocket (best druggability 0.45). MolNFT v1 #502409 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- P36218
- Type
- protein
- Length
- 229 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0A70d3367d1cE30ff1149924db0112B10f5dbed3
- Molecule
- Endo-1,4-beta-xylanase 1
- UniProt
- P36218
- Pockets
- 1 · best druggability 0.45
Structure
1 distinct chain · 4% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endo-1,4-beta-xylanase 1 | protein | 229 | 4% helix, 52% strand | P36218 |
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 | 100 | 0.45 | 0.79 | 18 | empty |
Compared structures
- 1XYN · Structural comparison of two major endo-1,4-beta-xylanases from trichodrema reesei · an experimental structure of the same protein · chain A against A, TM-score 0.78
- 1XYN · Structural comparison of two major endo-1,4-beta-xylanases from trichodrema reesei · an experimental structure of the same protein · chain A against A, TM-score 0.78
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 P36218
- Elsewhere: UniProt P36218 · AlphaFold DB P36218
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