Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (B5EBQ2)
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
- B5EBQ2
- Type
- protein
- Length
- 461 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x78Cc7f9BF18AF8279e492D45EE7Fe9d7cC6f6D07
- Molecule
- Udp-N-acetylmuramate--L-alanine ligase
- UniProt
- B5EBQ2
- Pockets
- 2 · best druggability 0.66
Structure
1 distinct chain · 36% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramate--L-alanine ligase | protein | 461 | 36% helix, 24% strand | B5EBQ2 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 523 | 0.66 | 0.77 | 55 | empty |
| 2 | 170 | 0.63 | 0.85 | 28 | 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 B5EBQ2
- Elsewhere: UniProt B5EBQ2 · AlphaFold DB B5EBQ2
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