Research workbench
AlphaFold monomer V2.0 prediction for udp-N- acetylenolpyruvoylglucosamine reductase (A5D143)
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
- A5D143
- Type
- protein
- Length
- 313 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x8edD144f4ac42c0531a333DF70DD4843E3D334A9
- Molecule
- Udp-N-acetylenolpyruvoylglucosamine reductase
- UniProt
- A5D143
- Pockets
- 2 · best druggability 0.76
Structure
1 distinct chain · 34% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylenolpyruvoylglucosamine reductase | protein | 313 | 34% helix, 26% strand | A5D143 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 547 | 0.76 | 0.84 | 74 | empty |
| 2 | 82 | 0.31 | 0.73 | 20 | 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 A5D143
- Elsewhere: UniProt A5D143 · AlphaFold DB A5D143
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