Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramoylalanine-- D-glutamate ligase (Q9RRJ4)
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
- Q9RRJ4
- Type
- protein
- Length
- 457 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x159a74F8323b2EB2cC088ac2b0e2E49Cd847Cacd
- Molecule
- Udp-N-acetylmuramoylalanine--D-glutamate ligase
- UniProt
- Q9RRJ4
- Pockets
- 4 · best druggability 0.72
Structure
1 distinct chain · 38% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramoylalanine--D-glutamate ligase | protein | 457 | 38% helix, 19% strand | Q9RRJ4 |
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 | 770 | 0.72 | 0.78 | 97 | empty |
| 2 | 106 | 0.43 | 0.78 | 18 | empty |
| 3 | 159 | 0.42 | 0.74 | 31 | empty |
| 4 | 77 | 0.31 | 0.73 | 22 | 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 Q9RRJ4
- Elsewhere: UniProt Q9RRJ4 · AlphaFold DB Q9RRJ4
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