Research workbench
Human muscle fructose-1,6-bisphosphatase in active R-state in complex with fructose-1,6-bisphosphate
Analyse Human muscle fructose-1,6-bisphosphatase in active R-state in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5K56
- Type
- protein
- Length
- 275 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.198
- Source
- Homo sapiens
- Molecule
- Fructose-1,6-bisphosphatase isozyme 2
- EC
- 3.1.3.11
- UniProt
- O00757
- Ligands
- FBP
- Pockets
- 2 · best druggability 0.37
Structure
x-ray diffraction · resolution 2.198 · 1 distinct chain · 36% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fructose-1,6-bisphosphatase isozyme 2 (EC 3.1.3.11) | protein | 275 | 36% helix, 27% strand | O00757 |
Ligands and binding sites
- FBP · 1,6-di-O-phosphono-beta-D-fructofuranose · sugar · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 88 | 0.37 | 0.76 | 19 | FBP |
| 2 | 91 | 0.34 | 0.74 | 16 | empty |
Compared structures
- 5K56 · Human muscle fructose-1,6-bisphosphatase in active R-state in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
- O00757 · AlphaFold monomer V2.0 prediction for fructose-1,6-bisphosphatase isozyme 2 (O00757) · 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 O00757
- Elsewhere: RCSB PDB 5K56 · PDBe 5K56 · UniProt O00757
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