Research workbench
Structure of the N-acetyltransferase domain of X. fastidiosa NAGS/K
Analyse Structure of the N-acetyltransferase domain of X. fastidiosa NAGS/K in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4NEX
- Type
- protein
- Length
- 303 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetylglutamate kinase
- EC
- 2.7.2.8
- UniProt
- Q87EL2
- Ligands
- NLG, SO4
- Pockets
- 2 · best druggability 0.66
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetylglutamate kinase (EC 2.7.2.8) | protein | 157 | 34% helix, 32% strand | Q87EL2 |
| B | Acetylglutamate kinase (EC 2.7.2.8) | protein | 146 | 36% helix, 30% strand | Q87EL2 |
Ligands and binding sites
- NLG · N-acetyl-L-glutamate · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 273 | 0.66 | 0.83 | 37 | NLG, SO4 |
| 2 | 136 | 0.64 | 0.87 | 21 | NLG |
Interfaces
1 interface between chains.
- A–B · 750 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 4NEX · Structure of the N-acetyltransferase domain of X. fastidiosa NAGS/K · the same entry in another collection · chain A against A, TM-score 1.00
- Q87EL2 · AlphaFold monomer V2.0 prediction for acetylglutamate kinase (Q87EL2) · a predicted model of the same protein · chain B against A, TM-score 0.97
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 Q87EL2
- Elsewhere: RCSB PDB 4NEX · PDBe 4NEX · UniProt Q87EL2
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