Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (Q7W4B5)
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
- Q7W4B5
- Type
- protein
- Length
- 468 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4351fbBA2D1ce306FC22A21df5a9787370D5053a
- Molecule
- Udp-N-acetylmuramate--L-alanine ligase
- UniProt
- Q7W4B5
- Pockets
- 4 · best druggability 0.73
Structure
1 distinct chain · 37% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramate--L-alanine ligase | protein | 468 | 37% helix, 26% strand | Q7W4B5 |
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 | 575 | 0.73 | 0.81 | 75 | empty |
| 2 | 63 | 0.34 | 0.77 | 16 | empty |
| 3 | 83 | 0.34 | 0.75 | 15 | empty |
| 4 | 50 | 0.33 | 0.79 | 16 | 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 Q7W4B5
- Elsewhere: UniProt Q7W4B5 · AlphaFold DB Q7W4B5
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