Research workbench
AlphaFold monomer V2.0 prediction for N-acetylmuramic acid 6-phosphate etherase (B1XMC7)
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
- B1XMC7
- Type
- protein
- Length
- 301 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xA94Fa173ae66BEB1f6B8a6F8f7C799dB208BC152
- Molecule
- N-acetylmuramic acid 6-phosphate etherase
- UniProt
- B1XMC7
- Pockets
- 2 · best druggability 0.52
Structure
1 distinct chain · 53% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-acetylmuramic acid 6-phosphate etherase | protein | 301 | 53% helix, 10% strand | B1XMC7 |
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 | 143 | 0.52 | 0.80 | 30 | empty |
| 2 | 198 | 0.45 | 0.73 | 30 | 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 B1XMC7
- Elsewhere: UniProt B1XMC7 · AlphaFold DB B1XMC7
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