Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramoylalanine-- D-glutamate ligase (A0M529)
Analyse AlphaFold monomer V2.0 prediction for udp-N-acetylmuramoylalanine-- D-glutamate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A0M529
- Type
- protein
- Length
- 445 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4d07E6a23DeB6B95bd9b90EcB67368b7e8D3B77e
- Molecule
- Udp-N-acetylmuramoylalanine--D-glutamate ligase
- UniProt
- A0M529
- Pockets
- 3 · best druggability 0.67
Structure
1 distinct chain · 38% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramoylalanine--D-glutamate ligase | protein | 445 | 38% helix, 23% strand | A0M529 |
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 | 398 | 0.67 | 0.80 | 44 | empty |
| 2 | 639 | 0.65 | 0.75 | 63 | empty |
| 3 | 56 | 0.29 | 0.75 | 13 | 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 A0M529
- Elsewhere: UniProt A0M529 · AlphaFold DB A0M529
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