Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (A9H0J3)
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
- A9H0J3
- Type
- protein
- Length
- 480 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x8216949dDEF9EaDBdB1a9037895912E009a911AA
- Molecule
- Udp-N-acetylmuramate--L-alanine ligase
- UniProt
- A9H0J3
- Pockets
- 4 · best druggability 0.74
Structure
1 distinct chain · 37% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramate--L-alanine ligase | protein | 480 | 37% helix, 25% strand | A9H0J3 |
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 | 791 | 0.74 | 0.79 | 87 | empty |
| 2 | 138 | 0.46 | 0.77 | 22 | empty |
| 3 | 85 | 0.39 | 0.78 | 14 | empty |
| 4 | 69 | 0.32 | 0.75 | 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 A9H0J3
- Elsewhere: UniProt A9H0J3 · AlphaFold DB A9H0J3
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