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AlphaFold monomer V2.0 prediction for udp-N-acetylglucosamine-- N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase (A7FM66)
Analyse AlphaFold monomer V2.0 prediction for udp-N-acetylglucosamine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A7FM66
- Type
- protein
- Length
- 356 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xF3b04d65F1aD0058771B149FB8BD62b3934a8918
- Molecule
- Udp-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol…
- UniProt
- A7FM66
- Pockets
- 2 · best druggability 0.69
Structure
1 distinct chain · 46% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase | protein | 356 | 46% helix, 15% strand | A7FM66 |
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 | 787 | 0.69 | 0.75 | 77 | empty |
| 2 | 54 | 0.49 | 0.86 | 18 | 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 A7FM66
- Elsewhere: UniProt A7FM66 · AlphaFold DB A7FM66
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