MolNFT v1 · #118148 · protein
Human muscle fructose-1,6-bisphosphatase in active R-state in complex with fructose-6-phosphate
5ET8 · Fructose-1,6-bisphosphatase isozyme 2: “Human muscle fructose-1,6-bisphosphatase in active R-state in complex with fructose-6-phosphate”. X-ray diffraction, 1 ligand (F6P), 2 pockets (best druggability 0.51). MolNFT v1 #118148 on…
- PDB
- 5ET8
- Type
- protein
- Length
- 287 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fructose-1,6-bisphosphatase isozyme 2
- EC
- 3.1.3.11
- UniProt
- O00757
- Ligands
- F6P
- Pockets
- 2 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fructose-1,6-bisphosphatase isozyme 2 (EC 3.1.3.11) | protein | 287 | 37% helix, 26% strand | O00757 |
Ligands and binding sites
- F6P · 6-O-phosphono-beta-D-fructofuranose · ligand · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 200 | 0.51 | 0.76 | 23 | empty |
| 2 | 70 | 0.32 | 0.75 | 17 | F6P |
Compared structures
- 5ET8 · 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 5ET8 · PDBe 5ET8 · UniProt O00757
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