Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (Q9RNM7)
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
- Q9RNM7
- Type
- protein
- Length
- 476 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xa73BAb1DabE4333A884D03393eAa10c3B4215494
- Molecule
- Udp-N-acetylmuramate--L-alanine ligase
- UniProt
- Q9RNM7
- Pockets
- 5 · best druggability 0.70
Structure
1 distinct chain · 37% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramate--L-alanine ligase | protein | 476 | 37% helix, 25% strand | Q9RNM7 |
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 | 789 | 0.70 | 0.76 | 70 | empty |
| 2 | 195 | 0.63 | 0.84 | 31 | empty |
| 3 | 187 | 0.48 | 0.76 | 26 | empty |
| 4 | 67 | 0.38 | 0.78 | 15 | empty |
| 5 | 110 | 0.35 | 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 Q9RNM7
- Elsewhere: UniProt Q9RNM7 · AlphaFold DB Q9RNM7
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