Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (A5CW53)
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
- A5CW53
- Type
- protein
- Length
- 469 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd6dAC69607350B6653b5aBcE7c26e6D0Da978570
- Molecule
- Udp-N-acetylmuramate--L-alanine ligase
- UniProt
- A5CW53
- Pockets
- 5 · best druggability 0.70
Structure
1 distinct chain · 38% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramate--L-alanine ligase | protein | 469 | 38% helix, 24% strand | A5CW53 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 740 | 0.70 | 0.77 | 61 | empty |
| 2 | 251 | 0.63 | 0.81 | 32 | empty |
| 3 | 156 | 0.47 | 0.76 | 18 | empty |
| 4 | 59 | 0.39 | 0.80 | 15 | empty |
| 5 | 56 | 0.31 | 0.76 | 12 | 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 A5CW53
- Elsewhere: UniProt A5CW53 · AlphaFold DB A5CW53
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