MolNFT v1 · #6854 · protein
Crystal structure of the neutral form of fructose 1,6-bisphosphatase complexed with regulatory inhibitor fructose 2,6-bisphosphate at 2.6- ångströms resolution
1FPB: “Crystal structure of the neutral form of fructose 1,6-bisphosphatase complexed with regulatory inhibitor…”. X-ray diffraction, 1 ligand (FDP), 8 pockets (best druggability 0.53). MolNFT v1 #6854 on GenesisL1: 3D structure, binding…
- PDB
- 1FPB
- Type
- protein
- Length
- 626 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
- FDP
- Pockets
- 8 · best druggability 0.53
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Fructose 1,6-bisphosphatase (EC 3.1.3.11) | protein | 313 | 35% helix, 26% strand | P00636 |
Ligands and binding sites
- FDP · 2,6-di-O-phosphono-beta-D-fructofuranose · ligand · 3 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 202 | 0.53 | 0.78 | 37 | FDP |
| 2 | 161 | 0.52 | 0.79 | 24 | FDP |
| 3 | 122 | 0.48 | 0.79 | 21 | FDP |
| 4 | 102 | 0.45 | 0.78 | 17 | empty |
| 5 | 117 | 0.43 | 0.77 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 2099 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 1FPB · Crystal structure of the neutral form of fructose 1,6-bisphosphatase complexed with… · 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 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 P00636
- Elsewhere: RCSB PDB 1FPB · PDBe 1FPB · UniProt P00636
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