Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (Q8DEL1)
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
- Q8DEL1
- Type
- protein
- Length
- 486 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x78Cc7f9BF18AF8279e492D45EE7Fe9d7cC6f6D07
- Molecule
- Udp-N-acetylmuramate--L-alanine ligase
- UniProt
- Q8DEL1
- Pockets
- 3 · best druggability 0.76
Structure
1 distinct chain · 37% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramate--L-alanine ligase | protein | 486 | 37% helix, 24% strand | Q8DEL1 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 864 | 0.76 | 0.79 | 88 | empty |
| 2 | 62 | 0.34 | 0.77 | 14 | empty |
| 3 | 93 | 0.31 | 0.73 | 18 | 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 Q8DEL1
- Elsewhere: UniProt Q8DEL1 · AlphaFold DB Q8DEL1
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