Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (B0CCD6)
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
- B0CCD6
- Type
- protein
- Length
- 487 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xF49216F986743596cFbee1Bb2e7b6F3AB486D836
- Molecule
- Udp-N-acetylmuramate--L-alanine ligase
- UniProt
- B0CCD6
- Pockets
- 3 · best druggability 0.75
Structure
1 distinct chain · 36% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramate--L-alanine ligase | protein | 487 | 36% helix, 23% strand | B0CCD6 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 869 | 0.75 | 0.79 | 68 | empty |
| 2 | 212 | 0.64 | 0.83 | 29 | empty |
| 3 | 91 | 0.38 | 0.76 | 22 | 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 B0CCD6
- Elsewhere: UniProt B0CCD6 · AlphaFold DB B0CCD6
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.