Research workbench
Glutaminase domain of glucosamine 6-phosphate synthase complexed with glutamate
Analyse Glutaminase domain of glucosamine 6-phosphate synthase complexed with glutamate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1XFF
- Type
- protein
- Length
- 477 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glucosamine--fructose-6-phosphate aminotransferase [isomerizing]
- EC
- 2.6.1.16
- UniProt
- P17169
- Ligands
- GLU, NA
- Pockets
- 3 · best druggability 0.40
Structure
x-ray diffraction · 2 distinct chains · 25% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glucosamine--fructose-6-phosphate aminotransferase [isomerizing] (EC 2.6.1.16) | protein | 238 | 26% helix, 34% strand | P17169 |
| B | Glucosamine--fructose-6-phosphate aminotransferase [isomerizing] (EC 2.6.1.16) | protein | 239 | 24% helix, 33% strand | P17169 |
Ligands and binding sites
- GLU · Glutamic acid · ligand · 2 copies · chains A, B
- NA · Sodium ion · metal · 2 copies · chains A, B
- ACT · Acetate ion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 94 | 0.40 | 0.78 | 22 | empty |
| 2 | 67 | 0.39 | 0.80 | 19 | GLU |
| 3 | 86 | 0.39 | 0.77 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 768 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 1XFF · Glutaminase domain of glucosamine 6-phosphate synthase complexed with glutamate · 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 0.99
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 1XFF · PDBe 1XFF · UniProt P17169
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