Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (Q8UDM9)
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
- Q8UDM9
- Type
- protein
- Length
- 471 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x8c3620A532877ca1BDf102CC1189355ACB69dc82
- Molecule
- Udp-N-acetylmuramate--L-alanine ligase
- UniProt
- Q8UDM9
- Pockets
- 4 · best druggability 0.67
Structure
1 distinct chain · 36% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramate--L-alanine ligase | protein | 471 | 36% helix, 26% strand | Q8UDM9 |
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 | 700 | 0.67 | 0.76 | 67 | empty |
| 2 | 229 | 0.60 | 0.81 | 32 | empty |
| 3 | 85 | 0.49 | 0.82 | 15 | empty |
| 4 | 57 | 0.32 | 0.76 | 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 Q8UDM9
- Elsewhere: UniProt Q8UDM9 · AlphaFold DB Q8UDM9
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