Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (B6ELH4)
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
- B6ELH4
- Type
- protein
- Length
- 487 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3c368827Ad0a22A7871F24e9Fd5d533A4cf73D7e
- Molecule
- Udp-N-acetylmuramate--L-alanine ligase
- UniProt
- B6ELH4
- Pockets
- 3 · best druggability 0.76
Structure
1 distinct chain · 38% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramate--L-alanine ligase | protein | 487 | 38% helix, 24% strand | B6ELH4 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 878 | 0.76 | 0.79 | 82 | empty |
| 2 | 57 | 0.31 | 0.76 | 12 | empty |
| 3 | 55 | 0.28 | 0.74 | 12 | 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 B6ELH4
- Elsewhere: UniProt B6ELH4 · AlphaFold DB B6ELH4
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