Research workbench
Fructose-1,6-bisphosphatase (D-fructose-1,6-bisphosphate 1- phosphohydrolase) complexed with AMP, 2,5-anhydro-D-glucitol-1,6- bisphosphate, thallium (10 mm) and lithium ions (10 mm)
Analyse Fructose-1,6-bisphosphatase (D-fructose-1,6-bisphosphate 1- phosphohydrolase)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FPJ
- Type
- protein
- Length
- 634 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fructose-1,6-bisphosphatase
- EC
- 3.1.3.11
- UniProt
- P00636
- Ligands
- AMP, AHG, TL
- Pockets
- 8 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Fructose-1,6-bisphosphatase (EC 3.1.3.11) | protein | 317 | 39% helix, 26% strand | P00636 |
Ligands and binding sites
- AMP · Adenosine monophosphate · ligand · 2 copies · chains A, B
- AHG · 2,5-anhydro-1,6-di-O-phosphono-D-glucitol · ligand · 2 copies · chains A, B
- TL · Thallium (I) ion · metal · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 231 | 0.57 | 0.79 | 42 | TL, AHG |
| 2 | 196 | 0.55 | 0.79 | 38 | TL, AHG |
| 3 | 156 | 0.51 | 0.79 | 21 | empty |
| 4 | 116 | 0.44 | 0.77 | 24 | empty |
| 5 | 122 | 0.43 | 0.76 | 19 | AMP |
Interfaces
1 interface between chains.
- A–B · 2339 Ų buried · 28 hydrogen bonds · protein-protein
Compared structures
- 1FPJ · Fructose-1,6-bisphosphatase (D-fructose-1,6-bisphosphate 1-phosphohydrolase) complexed… · the same entry in another collection · chain A against A, TM-score 1.00
- P00636 · AlphaFold monomer V2.0 prediction for fructose-1,6-bisphosphatase 1 (P00636) · a predicted model of the same protein · chain B against A, TM-score 0.97
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 P00636
- Elsewhere: RCSB PDB 1FPJ · PDBe 1FPJ · UniProt P00636
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