Research workbench
AlphaFold monomer V2.0 prediction for udp-N- acetylenolpyruvoylglucosamine reductase (P65461)
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
- P65461
- Type
- protein
- Length
- 369 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9e5E98E011361C5888c92e2CDb7652E02Bd5C7Ed
- Molecule
- Udp-N-acetylenolpyruvoylglucosamine reductase
- UniProt
- P65461
- Pockets
- 3 · best druggability 0.85
Structure
1 distinct chain · 26% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylenolpyruvoylglucosamine reductase | protein | 369 | 26% helix, 25% strand | P65461 |
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 | 830 | 0.85 | 0.87 | 85 | empty |
| 2 | 122 | 0.40 | 0.75 | 26 | empty |
| 3 | 107 | 0.37 | 0.74 | 22 | 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 P65461
- Elsewhere: UniProt P65461 · AlphaFold DB P65461
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