Research workbench
AlphaFold monomer V2.0 prediction for N-acetylmuramic acid 6-phosphate etherase (Q1AYD7)
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
- Q1AYD7
- Type
- protein
- Length
- 301 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x79a905d858Ce72991FD6E7a9C6498620f42E146D
- Molecule
- N-acetylmuramic acid 6-phosphate etherase
- UniProt
- Q1AYD7
- Pockets
- 4 · best druggability 0.40
Structure
1 distinct chain · 55% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-acetylmuramic acid 6-phosphate etherase | protein | 301 | 55% helix, 9% strand | Q1AYD7 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 113 | 0.40 | 0.76 | 20 | empty |
| 2 | 71 | 0.29 | 0.73 | 21 | empty |
| 3 | 68 | 0.28 | 0.73 | 13 | empty |
| 4 | 63 | 0.28 | 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 Q1AYD7
- Elsewhere: UniProt Q1AYD7 · AlphaFold DB Q1AYD7
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