Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylglucosamine 4,6-dehydratase (inverting) (Q0P8W4)
Analyse AlphaFold monomer V2.0 prediction for udp-N-acetylglucosamine 4,6-dehydratase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q0P8W4
- Type
- protein
- Length
- 334 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0D671490EE06E75975e90D7F99F73B20BE618744
- Molecule
- Udp-N-acetylglucosamine 4,6-dehydratase (inverting)
- UniProt
- Q0P8W4
- Pockets
- 3 · best druggability 0.80
Structure
1 distinct chain · 38% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylglucosamine 4,6-dehydratase (inverting) | protein | 334 | 38% helix, 21% strand | Q0P8W4 |
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 | 802 | 0.80 | 0.83 | 77 | empty |
| 2 | 58 | 0.47 | 0.84 | 19 | empty |
| 3 | 64 | 0.28 | 0.73 | 19 | 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 Q0P8W4
- Elsewhere: UniProt Q0P8W4 · AlphaFold DB Q0P8W4
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