Research workbench
AlphaFold monomer V2.0 prediction for N-acetylmuramic acid 6-phosphate etherase (C1KVV7)
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
- C1KVV7
- Type
- protein
- Length
- 296 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6227512B0B04f05c48A3f9Bb2A26C737dAb650E8
- Molecule
- N-acetylmuramic acid 6-phosphate etherase
- UniProt
- C1KVV7
- Pockets
- 2 · best druggability 0.33
Structure
1 distinct chain · 56% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-acetylmuramic acid 6-phosphate etherase | protein | 296 | 56% helix, 10% strand | C1KVV7 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 77 | 0.33 | 0.75 | 18 | empty |
| 2 | 68 | 0.31 | 0.75 | 17 | 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 C1KVV7
- Elsewhere: UniProt C1KVV7 · AlphaFold DB C1KVV7
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