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AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (A1UTC4)
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
- A1UTC4
- Type
- protein
- Length
- 475 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5c4adF1416281C09AE8eE1cbb80fF7e44cE86F97
- Molecule
- Udp-N-acetylmuramate--L-alanine ligase
- UniProt
- A1UTC4
- Pockets
- 2 · best druggability 0.75
Structure
1 distinct chain · 36% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramate--L-alanine ligase | protein | 475 | 36% helix, 26% strand | A1UTC4 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 977 | 0.75 | 0.78 | 87 | empty |
| 2 | 119 | 0.44 | 0.77 | 17 | 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 A1UTC4
- Elsewhere: UniProt A1UTC4 · AlphaFold DB A1UTC4
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