Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramoylalanine-- D-glutamate ligase (Q5NHK3)
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
- Q5NHK3
- Type
- protein
- Length
- 416 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xdF2b063d4B94F3f46D117B1af99A846bD4a59284
- Molecule
- Udp-N-acetylmuramoylalanine--D-glutamate ligase
- UniProt
- Q5NHK3
- Pockets
- 4 · best druggability 0.71
Structure
1 distinct chain · 38% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramoylalanine--D-glutamate ligase | protein | 416 | 38% helix, 26% strand | Q5NHK3 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 484 | 0.71 | 0.81 | 59 | empty |
| 2 | 139 | 0.53 | 0.81 | 21 | empty |
| 3 | 171 | 0.51 | 0.78 | 23 | empty |
| 4 | 214 | 0.50 | 0.76 | 29 | 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 Q5NHK3
- Elsewhere: UniProt Q5NHK3 · AlphaFold DB Q5NHK3
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