Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (B4SJX6)
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
- B4SJX6
- Type
- protein
- Length
- 478 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xE56999B39685E9b46FBc6B6E6714a8DC44B1B732
- Molecule
- Udp-N-acetylmuramate--L-alanine ligase
- UniProt
- B4SJX6
- Pockets
- 4 · best druggability 0.74
Structure
1 distinct chain · 37% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramate--L-alanine ligase | protein | 478 | 37% helix, 24% strand | B4SJX6 |
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 | 753 | 0.74 | 0.80 | 80 | empty |
| 2 | 170 | 0.56 | 0.80 | 24 | empty |
| 3 | 55 | 0.30 | 0.76 | 17 | empty |
| 4 | 51 | 0.29 | 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 B4SJX6
- Elsewhere: UniProt B4SJX6 · AlphaFold DB B4SJX6
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