Research workbench
Crystal structure of native MMNAGS/K
Analyse Crystal structure of native MMNAGS/K in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3S6H
- Type
- protein
- Length
- 1,714 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-acetylglutamate kinase / N-acetylglutamate synthase
- EC
- 2.3.1.1, 2.7.2.8
- UniProt
- Q0ASS9
- Ligands
- GLU, COA
- Pockets
- 20 · best druggability 0.83
Structure
x-ray diffraction · 3 distinct chains · 36% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-acetylglutamate kinase / N-acetylglutamate synthase (EC 2.3.1.1, 2.7.2.8) | protein | 436 | 40% helix, 21% strand | Q0ASS9 |
| B, X | N-acetylglutamate kinase / N-acetylglutamate synthase (EC 2.3.1.1, 2.7.2.8) | protein | 435 | 34% helix, 22% strand | Q0ASS9 |
| Y | N-acetylglutamate kinase / N-acetylglutamate synthase (EC 2.3.1.1, 2.7.2.8) | protein | 408 | 35% helix, 22% strand | Q0ASS9 |
Ligands and binding sites
- GLU · Glutamic acid · ligand · 2 copies · chains A, Y
- COA · Coenzyme A · ligand · 2 copies · chains A, X, B, Y
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 995 | 0.83 | 0.84 | 128 | empty |
| 2 | 259 | 0.79 | 0.92 | 50 | empty |
| 3 | 981 | 0.77 | 0.79 | 99 | GLU |
| 4 | 149 | 0.74 | 0.93 | 35 | empty |
| 5 | 525 | 0.67 | 0.78 | 62 | empty |
Interfaces
5 interfaces between chains.
- A–X · 1586 Ų buried · 14 hydrogen bonds · protein-protein
- B–Y · 1187 Ų buried · 7 hydrogen bonds · protein-protein
- X–Y · 1074 Ų buried · 21 hydrogen bonds · protein-protein
- A–B · 1001 Ų buried · 16 hydrogen bonds · protein-protein
- B–X · 32 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 3S6H · Crystal structure of native mmNAGS/k · the same entry in another collection · chain A against A, TM-score 1.00
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 Q0ASS9
- Elsewhere: RCSB PDB 3S6H · PDBe 3S6H · UniProt Q0ASS9
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