Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetyl-D-mannosaminuronic acid transferase (B7L953)
Analyse AlphaFold monomer V2.0 prediction for udp-N-acetyl-D-mannosaminuronic acid… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B7L953
- Type
- protein
- Length
- 246 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0D671490EE06E75975e90D7F99F73B20BE618744
- Molecule
- Udp-N-acetyl-D-mannosaminuronic acid transferase
- UniProt
- B7L953
- Pockets
- 2 · best druggability 0.75
Structure
1 distinct chain · 52% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetyl-D-mannosaminuronic acid transferase | protein | 246 | 52% helix, 15% strand | B7L953 |
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 | 699 | 0.75 | 0.80 | 55 | empty |
| 2 | 52 | 0.26 | 0.73 | 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 B7L953
- Elsewhere: UniProt B7L953 · AlphaFold DB B7L953
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