Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (B7UZI9)
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
- B7UZI9
- Type
- protein
- Length
- 480 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x58f547A730085a8675d05778EcA28963bCE2dbA7
- Molecule
- Udp-N-acetylmuramate--L-alanine ligase
- UniProt
- B7UZI9
- Pockets
- 3 · best druggability 0.75
Structure
1 distinct chain · 34% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramate--L-alanine ligase | protein | 480 | 34% helix, 25% strand | B7UZI9 |
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 | 743 | 0.75 | 0.80 | 76 | empty |
| 2 | 190 | 0.62 | 0.83 | 30 | empty |
| 3 | 122 | 0.37 | 0.74 | 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 B7UZI9
- Elsewhere: UniProt B7UZI9 · AlphaFold DB B7UZI9
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