Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (C1DQA0)
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
- C1DQA0
- Type
- protein
- Length
- 488 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x2282b24c89f1D92FfBa894BD9f18ab55a2872194
- Molecule
- Udp-N-acetylmuramate--L-alanine ligase
- UniProt
- C1DQA0
- Pockets
- 4 · best druggability 0.74
Structure
1 distinct chain · 36% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramate--L-alanine ligase | protein | 488 | 36% helix, 24% strand | C1DQA0 |
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 | 828 | 0.74 | 0.79 | 84 | empty |
| 2 | 64 | 0.53 | 0.87 | 18 | empty |
| 3 | 55 | 0.37 | 0.80 | 13 | empty |
| 4 | 56 | 0.27 | 0.73 | 9 | 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 C1DQA0
- Elsewhere: UniProt C1DQA0 · AlphaFold DB C1DQA0
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