Research workbench
T-like fructose-1,6-bisphosphatase from escherichia COLI with AMP, glucose 6-phosphate, and fructose 1,6-bisphosphate bound
Analyse T-like fructose-1,6-bisphosphatase from escherichia COLI with AMP, glucose… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Q8M
- Type
- protein
- Length
- 620 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fructose-bisphosphatase
- EC
- 3.1.3.11
- UniProt
- Q31TG8
- Ligands
- FBP, AMP, BG6, MG, CL
- Pockets
- 7 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Fructose-bisphosphatase (EC 3.1.3.11) | protein | 310 | 36% helix, 24% strand | Q31TG8 |
Ligands and binding sites
- FBP · 1,6-di-O-phosphono-beta-D-fructofuranose · ligand · 2 copies · chains A, B
- AMP · Adenosine monophosphate · ligand · 2 copies · chains A, B
- BG6 · 6-O-phosphono-beta-D-glucopyranose · sugar · chains A
- MG · Magnesium ion · metal · 4 copies · chains A, B
- CL · Chloride ion · ion · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 505 | 0.74 | 0.83 | 55 | CL |
| 2 | 133 | 0.53 | 0.81 | 22 | AMP |
| 3 | 125 | 0.52 | 0.81 | 20 | AMP |
| 4 | 150 | 0.52 | 0.80 | 29 | FBP |
| 5 | 114 | 0.44 | 0.78 | 24 | FBP, MG |
Interfaces
1 interface between chains.
- A–B · 686 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 modified (engineered).
Compared structures
- 2Q8M · T-like Fructose-1,6-bisphosphatase from Escherichia coli with AMP, Glucose 6-phosphate… · the same entry in another collection · chain A against A, TM-score 1.00
- Q31TG8 · AlphaFold monomer V2.0 prediction for fructose-1,6-bisphosphatase class 1 (Q31TG8) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q31TG8
- Elsewhere: RCSB PDB 2Q8M · PDBe 2Q8M · UniProt Q31TG8
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