Research workbench
AlphaFold monomer V2.0 prediction for N-acetylglucosaminyldiphosphoundecaprenol N-acetyl-beta-D- mannosaminyltransferase (Q6GBJ4)
Analyse AlphaFold monomer V2.0 prediction for N-acetylglucosaminyldiphosphoundecaprenol… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q6GBJ4
- Type
- protein
- Length
- 254 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0cC2AEeb66a4ee22dDdd908c0A663C8De1D2D3e7
- Molecule
- N-acetylglucosaminyldiphosphoundecaprenol N-acetyl-beta-D- mannosaminyltransferase
- UniProt
- Q6GBJ4
- Pockets
- 2 · best druggability 0.78
Structure
1 distinct chain · 52% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-acetylglucosaminyldiphosphoundecaprenol N-acetyl-beta-D- mannosaminyltransferase | protein | 254 | 52% helix, 15% strand | Q6GBJ4 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 501 | 0.78 | 0.85 | 57 | empty |
| 2 | 240 | 0.62 | 0.81 | 22 | 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 Q6GBJ4
- Elsewhere: UniProt Q6GBJ4 · AlphaFold DB Q6GBJ4
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