MolNFT v1 · #502544 · protein
AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase C (Q9UV68)
Q9UV68: “AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase C (Q9UV68)”. 3 pockets (best druggability 0.53). MolNFT v1 #502544 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- Q9UV68
- Type
- protein
- Length
- 485 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0F7aAe0F58509eB3BaA013d642d748C7C38B0F93
- Molecule
- Endo-1,4-beta-xylanase C
- UniProt
- Q9UV68
- Pockets
- 3 · best druggability 0.53
Structure
1 distinct chain · 5% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endo-1,4-beta-xylanase C | protein | 485 | 5% helix, 34% strand | Q9UV68 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 263 | 0.53 | 0.76 | 45 | empty |
| 2 | 168 | 0.46 | 0.76 | 29 | empty |
| 3 | 104 | 0.39 | 0.76 | 30 | empty |
Modifications
Observed in the structure: 5 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 Q9UV68
- Elsewhere: UniProt Q9UV68 · AlphaFold DB Q9UV68
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