Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylglucosamine-- N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase (Q1MPB9)
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
- Q1MPB9
- Type
- protein
- Length
- 363 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x52E3CDE9815A62B85857BFe668884c9Bb2099566
- Molecule
- Udp-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol…
- UniProt
- Q1MPB9
- Pockets
- 3 · best druggability 0.75
Structure
1 distinct chain · 47% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase | protein | 363 | 47% helix, 16% strand | Q1MPB9 |
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 | 761 | 0.75 | 0.80 | 70 | empty |
| 2 | 87 | 0.48 | 0.82 | 20 | empty |
| 3 | 59 | 0.34 | 0.77 | 12 | 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 Q1MPB9
- Elsewhere: UniProt Q1MPB9 · AlphaFold DB Q1MPB9
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