Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (A1SU20)
Analyse AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A1SU20
- Type
- protein
- Length
- 487 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x1877Ad840Fa4414E25a1d686021eA644bBcE92D5
- Molecule
- Udp-N-acetylmuramate--L-alanine ligase
- UniProt
- A1SU20
- Pockets
- 4 · best druggability 0.75
Structure
1 distinct chain · 38% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramate--L-alanine ligase | protein | 487 | 38% helix, 24% strand | A1SU20 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 938 | 0.75 | 0.78 | 87 | empty |
| 2 | 75 | 0.33 | 0.75 | 19 | empty |
| 3 | 52 | 0.31 | 0.77 | 13 | empty |
| 4 | 57 | 0.30 | 0.75 | 15 | 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 A1SU20
- Elsewhere: UniProt A1SU20 · AlphaFold DB A1SU20
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