Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (A9WRD7)
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
- A9WRD7
- Type
- protein
- Length
- 465 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xEA023C66b29A57D0c10ab559620011c8b4d0C9bF
- Molecule
- Udp-N-acetylmuramate--L-alanine ligase
- UniProt
- A9WRD7
- Pockets
- 4 · best druggability 0.67
Structure
1 distinct chain · 37% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramate--L-alanine ligase | protein | 465 | 37% helix, 23% strand | A9WRD7 |
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 | 501 | 0.67 | 0.78 | 49 | empty |
| 2 | 208 | 0.65 | 0.84 | 30 | empty |
| 3 | 50 | 0.33 | 0.79 | 14 | empty |
| 4 | 66 | 0.31 | 0.74 | 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 A9WRD7
- Elsewhere: UniProt A9WRD7 · AlphaFold DB A9WRD7
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