Research workbench
AlphaFold monomer V2.0 prediction for udp-N- acetylenolpyruvoylglucosamine reductase (A9NA46)
Analyse AlphaFold monomer V2.0 prediction for udp-N- acetylenolpyruvoylglucosamine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A9NA46
- Type
- protein
- Length
- 316 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x35CE9E273dC599B97173f7Fa74880CacB153321E
- Molecule
- Udp-N-acetylenolpyruvoylglucosamine reductase
- UniProt
- A9NA46
- Pockets
- 3 · best druggability 0.74
Structure
1 distinct chain · 29% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylenolpyruvoylglucosamine reductase | protein | 316 | 29% helix, 27% strand | A9NA46 |
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 | 585 | 0.74 | 0.81 | 59 | empty |
| 2 | 154 | 0.49 | 0.77 | 19 | empty |
| 3 | 163 | 0.43 | 0.74 | 31 | 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 A9NA46
- Elsewhere: UniProt A9NA46 · AlphaFold DB A9NA46
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