Research workbench
Structure of human liver fbpase complexed with potent benzoxazole allosteric inhibitors
Analyse Structure of human liver fbpase complexed with potent benzoxazole allosteric… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2FIE
- Type
- protein
- Length
- 1,272 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fructose-1,6-bisphosphatase 1
- EC
- 3.1.3.11
- Ligands
- A74
- Pockets
- 18 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D, H, L | Fructose-1,6-bisphosphatase 1 (EC 3.1.3.11) | protein | 318 | 37% helix, 25% strand | — |
Ligands and binding sites
- A74 · 2,5-dichloro-N-[5-methoxy-7-(6-methoxypyridin-3-yl)-1,3-benzoxazol-2-yl]benzenesulfonamide · ligand · 4 copies · chains A, L, D, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
18 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1041 | 0.84 | 0.85 | 96 | empty |
| 2 | 426 | 0.68 | 0.80 | 45 | A74 |
| 3 | 394 | 0.66 | 0.79 | 53 | A74 |
| 4 | 206 | 0.64 | 0.84 | 56 | empty |
| 5 | 128 | 0.49 | 0.79 | 20 | empty |
Interfaces
6 interfaces between chains.
- H–L · 2391 Ų buried · 34 hydrogen bonds · protein-protein
- A–D · 2375 Ų buried · 32 hydrogen bonds · protein-protein
- A–L · 1279 Ų buried · 21 hydrogen bonds · protein-protein
- D–H · 1274 Ų buried · 27 hydrogen bonds · protein-protein
- D–L · 430 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 2FIE · Structure of human liver FBPase complexed with potent benzoxazole allosteric inhibitors · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 2FIE · PDBe 2FIE
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