Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetyl-D-mannosamine dehydrogenase (Q9L6R4)
Analyse AlphaFold monomer V2.0 prediction for udp-N-acetyl-D-mannosamine dehydrogenase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9L6R4
- Type
- protein
- Length
- 420 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x661f92Fc5950020C7aB410B5F5b9a3f429F49Ae5
- Molecule
- Udp-N-acetyl-D-mannosamine dehydrogenase
- UniProt
- Q9L6R4
- Pockets
- 4 · best druggability 0.66
Structure
1 distinct chain · 44% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetyl-D-mannosamine dehydrogenase | protein | 420 | 44% helix, 14% strand | Q9L6R4 |
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 | 327 | 0.66 | 0.81 | 46 | empty |
| 2 | 299 | 0.62 | 0.79 | 35 | empty |
| 3 | 166 | 0.49 | 0.77 | 26 | empty |
| 4 | 130 | 0.40 | 0.74 | 25 | 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 Q9L6R4
- Elsewhere: UniProt Q9L6R4 · AlphaFold DB Q9L6R4
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