MolNFT v1 · #250961 · protein
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (A0M526)
A0M526: “AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (A0M526)”. 2 pockets (best druggability 0.78). MolNFT v1 #250961 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- A0M526
- Type
- protein
- Length
- 452 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x8B076cFcCce75c7d28db718CD81F3160E1E1Ee20
- Molecule
- Udp-N-acetylmuramate--L-alanine ligase
- UniProt
- A0M526
- Pockets
- 2 · best druggability 0.78
Structure
1 distinct chain · 37% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramate--L-alanine ligase | protein | 452 | 37% helix, 26% strand | A0M526 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1159 | 0.78 | 0.80 | 68 | empty |
| 2 | 152 | 0.60 | 0.84 | 26 | 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 A0M526
- Elsewhere: UniProt A0M526 · AlphaFold DB A0M526
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