Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramoylalanine-- D-glutamate ligase (A4XI02)
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
- A4XI02
- Type
- protein
- Length
- 453 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6DAA77C4263E74E745cA9c4D8E291e57e8991Cf5
- Molecule
- Udp-N-acetylmuramoylalanine--D-glutamate ligase
- UniProt
- A4XI02
- Pockets
- 2 · best druggability 0.69
Structure
1 distinct chain · 37% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramoylalanine--D-glutamate ligase | protein | 453 | 37% helix, 23% strand | A4XI02 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 950 | 0.69 | 0.74 | 92 | empty |
| 2 | 143 | 0.44 | 0.76 | 19 | 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 A4XI02
- Elsewhere: UniProt A4XI02 · AlphaFold DB A4XI02
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