MolNFT v1 · #250757 · protein
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (Q6G125)
Q6G125: “AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (Q6G125)”. 3 pockets (best druggability 0.68). MolNFT v1 #250757 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- Q6G125
- Type
- protein
- Length
- 475 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9130a41bCa92dF77878ec5A9328e3D47AA08B359
- Molecule
- Udp-N-acetylmuramate--L-alanine ligase
- UniProt
- Q6G125
- Pockets
- 3 · best druggability 0.68
Structure
1 distinct chain · 36% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramate--L-alanine ligase | protein | 475 | 36% helix, 25% strand | Q6G125 |
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 | 582 | 0.68 | 0.77 | 47 | empty |
| 2 | 233 | 0.62 | 0.81 | 28 | empty |
| 3 | 75 | 0.38 | 0.78 | 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 Q6G125
- Elsewhere: UniProt Q6G125 · AlphaFold DB Q6G125
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