MolNFT v1 · #250732 · protein
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (A8HZ95)
A8HZ95: “AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (A8HZ95)”. 3 pockets (best druggability 0.74). MolNFT v1 #250732 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- A8HZ95
- Type
- protein
- Length
- 467 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9B130d619fCFc21d0D08E5Ce38Cf42A5fbe230CB
- Molecule
- Udp-N-acetylmuramate--L-alanine ligase
- UniProt
- A8HZ95
- Pockets
- 3 · best druggability 0.74
Structure
1 distinct chain · 36% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramate--L-alanine ligase | protein | 467 | 36% helix, 25% strand | A8HZ95 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 879 | 0.74 | 0.78 | 85 | empty |
| 2 | 50 | 0.32 | 0.77 | 13 | empty |
| 3 | 50 | 0.26 | 0.74 | 17 | 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 A8HZ95
- Elsewhere: UniProt A8HZ95 · AlphaFold DB A8HZ95
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