Research workbench
AlphaFold monomer V2.0 prediction for N-acetylmuramic acid 6-phosphate etherase 1 (Q838I8)
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
- Q838I8
- Type
- protein
- Length
- 300 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xa73BAb1DabE4333A884D03393eAa10c3B4215494
- Molecule
- N-acetylmuramic acid 6-phosphate etherase 1
- UniProt
- Q838I8
- Pockets
- 3 · best druggability 0.47
Structure
1 distinct chain · 56% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-acetylmuramic acid 6-phosphate etherase 1 | protein | 300 | 56% helix, 9% strand | Q838I8 |
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 | 169 | 0.47 | 0.76 | 28 | empty |
| 2 | 175 | 0.44 | 0.74 | 27 | empty |
| 3 | 72 | 0.30 | 0.73 | 15 | 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 Q838I8
- Elsewhere: UniProt Q838I8 · AlphaFold DB Q838I8
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