Research workbench
AlphaFold monomer V2.0 prediction for N-acylglucosamine 2-epimerase (P51606)
Analyse AlphaFold monomer V2.0 prediction for N-acylglucosamine 2-epimerase (P51606) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P51606
- Type
- protein
- Length
- 427 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x2aCAbD160b7F38A70125176a35A1a01870FE1a44
- Molecule
- N-acylglucosamine 2-epimerase
- UniProt
- P51606
- Pockets
- 4 · best druggability 0.70
Structure
1 distinct chain · 56% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-acylglucosamine 2-epimerase | protein | 427 | 56% helix, 9% strand | P51606 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 585 | 0.70 | 0.78 | 56 | empty |
| 2 | 162 | 0.52 | 0.79 | 26 | empty |
| 3 | 59 | 0.41 | 0.81 | 12 | empty |
| 4 | 101 | 0.38 | 0.75 | 14 | 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 P51606
- Elsewhere: UniProt P51606 · AlphaFold DB P51606
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