Research workbench
Glucosamine 6-phosphate synthase with glucose 6-phosphate
Analyse Glucosamine 6-phosphate synthase with glucose 6-phosphate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1JXA
- Type
- protein
- Length
- 1,824 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glucosamine 6-phosphate synthase
- EC
- 2.6.1.16
- UniProt
- P17169
- Ligands
- G6Q
- Pockets
- 16 · best druggability 0.87
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Glucosamine 6-phosphate synthase (EC 2.6.1.16) | protein | 608 | 35% helix, 18% strand | P17169 |
Ligands and binding sites
- G6Q · Glucose-6-phosphate · ligand · 2 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 659 | 0.87 | 0.92 | 64 | empty |
| 2 | 914 | 0.78 | 0.81 | 100 | empty |
| 3 | 114 | 0.76 | 0.96 | 28 | G6Q |
| 4 | 70 | 0.72 | 0.97 | 24 | empty |
| 5 | 306 | 0.71 | 0.85 | 42 | empty |
Interfaces
1 interface between chains.
- B–C · 3057 Ų buried · 38 hydrogen bonds · protein-protein
Compared structures
- 1JXA · Glucosamine 6-phosphate synthase with glucose 6-phosphate · the same entry in another collection · chain A against A, TM-score 1.00
- P17169 · AlphaFold monomer V2.0 prediction for glutamine--fructose-6-phosphate aminotransferase… · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P17169
- Elsewhere: RCSB PDB 1JXA · PDBe 1JXA · UniProt P17169
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