Research workbench
AlphaFold monomer V2.0 prediction for N-acetylmuramic acid 6-phosphate etherase (Q040J1)
Analyse AlphaFold monomer V2.0 prediction for N-acetylmuramic acid 6-phosphate etherase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q040J1
- Type
- protein
- Length
- 297 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0D671490EE06E75975e90D7F99F73B20BE618744
- Molecule
- N-acetylmuramic acid 6-phosphate etherase
- UniProt
- Q040J1
- Pockets
- 3 · best druggability 0.38
Structure
1 distinct chain · 58% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-acetylmuramic acid 6-phosphate etherase | protein | 297 | 58% helix, 10% strand | Q040J1 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 95 | 0.38 | 0.76 | 22 | empty |
| 2 | 50 | 0.26 | 0.74 | 19 | empty |
| 3 | 50 | 0.23 | 0.71 | 11 | 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 Q040J1
- Elsewhere: UniProt Q040J1 · AlphaFold DB Q040J1
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