Research workbench
AlphaFold monomer V2.0 prediction for udp-N- acetylenolpyruvoylglucosamine reductase (A1KFV6)
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
- A1KFV6
- Type
- protein
- Length
- 369 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x362a6d063b1B7E1B6EfD3A9A7CA3612e3FE037AA
- Molecule
- Udp-N-acetylenolpyruvoylglucosamine reductase
- UniProt
- A1KFV6
- Pockets
- 3 · best druggability 0.83
Structure
1 distinct chain · 27% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylenolpyruvoylglucosamine reductase | protein | 369 | 27% helix, 26% strand | A1KFV6 |
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 | 746 | 0.83 | 0.87 | 74 | empty |
| 2 | 114 | 0.37 | 0.74 | 26 | empty |
| 3 | 91 | 0.33 | 0.73 | 21 | 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 A1KFV6
- Elsewhere: UniProt A1KFV6 · AlphaFold DB A1KFV6
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