MolNFT v2 · #124452 · protein
Human muscle fructose-1,6-bisphosphatase in active R-state in complex with fructose-1,6-bisphosphate
5K56: “Human muscle fructose-1,6-bisphosphatase in active R-state in complex with fructose-1,6-bisphosphate”. X-ray diffraction at 2.198, 1 ligand (FBP). MolNFT v2 #124452 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- 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
- UniProt
- O00757
- Ligands
- FBP
Structure
x-ray diffraction · resolution 2.198 · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 275 | — | 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.
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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