Research workbench
Human liver fructose-1,6-bisphosphatase 1 (fructose 1,6-bisphosphate 1-phosphatase, E.C.3.1.3.11) complexed with the allosteric inhibitor 1-(1-benzothiophen-3-ylsulfonyl)-3-(5-bromo-1,3-thiazol-2-YL)UREA
Analyse Human liver fructose-1,6-bisphosphatase 1 (fructose 1,6-bisphosphate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5Q08
- Type
- protein
- Length
- 2,542 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fructose-1,6-bisphosphatase 1
- EC
- 3.1.3.11
- UniProt
- Q2TU34
- Ligands
- 967
- Pockets
- 20 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D, E | Fructose-1,6-bisphosphatase 1 (EC 3.1.3.11) | protein | 319 | 39% helix, 24% strand | Q2TU34 |
| B, C, F, G, H | Fructose-1,6-bisphosphatase 1 (EC 3.1.3.11) | protein | 317 | 39% helix, 24% strand | Q2TU34 |
Ligands and binding sites
- 967 · N-[(5-bromo-1,3-thiazol-2-yl)carbamoyl]-1-benzothiophene-3-sulfonamide · ligand · 8 copies · chains A, C, B, D, E, G, F, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1156 | 0.83 | 0.84 | 105 | empty |
| 2 | 1200 | 0.83 | 0.84 | 117 | empty |
| 3 | 503 | 0.69 | 0.79 | 58 | empty |
| 4 | 371 | 0.67 | 0.81 | 72 | empty |
| 5 | 387 | 0.66 | 0.80 | 45 | 967 |
Interfaces
14 interfaces between chains.
- A–B · 2398 Ų buried · 31 hydrogen bonds · protein-protein
- G–H · 2350 Ų buried · 30 hydrogen bonds · protein-protein
- C–D · 2349 Ų buried · 31 hydrogen bonds · protein-protein
- E–F · 2331 Ų buried · 31 hydrogen bonds · protein-protein
- F–H · 1313 Ų buried · 28 hydrogen bonds · protein-protein
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 Q2TU34
- Elsewhere: RCSB PDB 5Q08 · PDBe 5Q08 · UniProt Q2TU34
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