Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (Q1G9A0)
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
- Q1G9A0
- Type
- protein
- Length
- 439 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7624F52aB4e3B3130675848B7a6E7d66e4F77F72
- Molecule
- Udp-N-acetylmuramate--L-alanine ligase
- UniProt
- Q1G9A0
- Pockets
- 3 · best druggability 0.68
Structure
1 distinct chain · 35% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramate--L-alanine ligase | protein | 439 | 35% helix, 25% strand | Q1G9A0 |
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 | 614 | 0.68 | 0.77 | 55 | empty |
| 2 | 278 | 0.67 | 0.83 | 45 | empty |
| 3 | 71 | 0.30 | 0.73 | 18 | 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 Q1G9A0
- Elsewhere: UniProt Q1G9A0 · AlphaFold DB Q1G9A0
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