MolNFT v1 · #250959 · protein
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (Q5FUJ4)
Q5FUJ4: “AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (Q5FUJ4)”. 4 pockets (best druggability 0.72). MolNFT v1 #250959 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- Q5FUJ4
- Type
- protein
- Length
- 477 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4d07E6a23DeB6B95bd9b90EcB67368b7e8D3B77e
- Molecule
- Udp-N-acetylmuramate--L-alanine ligase
- UniProt
- Q5FUJ4
- Pockets
- 4 · best druggability 0.72
Structure
1 distinct chain · 36% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramate--L-alanine ligase | protein | 477 | 36% helix, 25% strand | Q5FUJ4 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 713 | 0.72 | 0.79 | 70 | empty |
| 2 | 115 | 0.43 | 0.77 | 20 | empty |
| 3 | 115 | 0.41 | 0.76 | 16 | empty |
| 4 | 85 | 0.35 | 0.75 | 13 | 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 Q5FUJ4
- Elsewhere: UniProt Q5FUJ4 · AlphaFold DB Q5FUJ4
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