Research workbench
Structure of the Class II Fructose-1,6-Bisphophatase from Francisella tularensis
Analyse Structure of the Class II Fructose-1,6-Bisphophatase from Francisella tularensis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7JS3
- Type
- protein
- Length
- 1,300 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.4
- Source
- Francisella tularensis
- Molecule
- Fructose-1,6-bisphosphatase
- UniProt
- A0A0E2ZJY0
- Ligands
- MG
- Pockets
- 20 · best druggability 0.84
Structure
x-ray diffraction · resolution 2.4 · 1 distinct chain · 32% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Fructose-1,6-bisphosphatase | protein | 325 | 32% helix, 30% strand | A0A0E2ZJY0 |
Ligands and binding sites
- MG · Magnesium ion · metal · 4 copies · chains A, B, C
- GOL · Glycerol · additive · 6 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 637 | 0.84 | 0.89 | 90 | GOL |
| 2 | 780 | 0.84 | 0.87 | 105 | empty |
| 3 | 261 | 0.73 | 0.87 | 48 | empty |
| 4 | 231 | 0.56 | 0.78 | 38 | empty |
| 5 | 319 | 0.56 | 0.76 | 37 | MG |
Interfaces
6 interfaces between chains.
- A–B · 1573 Ų buried · 32 hydrogen bonds · protein-protein
- C–D · 1540 Ų buried · 27 hydrogen bonds · protein-protein
- A–D · 1534 Ų buried · 32 hydrogen bonds · protein-protein
- B–C · 1438 Ų buried · 30 hydrogen bonds · protein-protein
- A–C · 126 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 7JS3 · Structure of the class II fructose-1,6-bisphophatase from francisella tularensis · 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 A0A0E2ZJY0
- Elsewhere: RCSB PDB 7JS3 · PDBe 7JS3 · UniProt A0A0E2ZJY0
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