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 [5-[2-amino-5-(2-methylpropyl)-1,3-thiazol-4-YL]FURAN-2-YL]PHOSPHONIC acid
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
- 5PZU
- Type
- protein
- Length
- 1,271 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
- UniProt
- Q2TU34
- Ligands
- 94D
- Pockets
- 20 · best druggability 0.82
Structure
x-ray diffraction · 3 distinct chains · 39% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fructose-1,6-bisphosphatase 1 (EC 3.1.3.11) | protein | 319 | 39% helix, 24% strand | Q2TU34 |
| B, D | Fructose-1,6-bisphosphatase 1 (EC 3.1.3.11) | protein | 317 | 39% helix, 25% strand | Q2TU34 |
| C | Fructose-1,6-bisphosphatase 1 (EC 3.1.3.11) | protein | 318 | 39% helix, 24% strand | Q2TU34 |
Ligands and binding sites
- 94D · {5-[2-amino-5-(2-methylpropyl)-1,3-thiazol-4-yl]furan-2-yl}phosphonic acid · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 847 | 0.82 | 0.85 | 92 | empty |
| 2 | 664 | 0.68 | 0.76 | 73 | empty |
| 3 | 342 | 0.65 | 0.80 | 63 | empty |
| 4 | 59 | 0.62 | 0.92 | 32 | empty |
| 5 | 310 | 0.61 | 0.78 | 37 | empty |
Interfaces
6 interfaces between chains.
- A–B · 2382 Ų buried · 32 hydrogen bonds · protein-protein
- C–D · 2381 Ų buried · 31 hydrogen bonds · protein-protein
- B–D · 1265 Ų buried · 32 hydrogen bonds · protein-protein
- A–C · 1250 Ų buried · 30 hydrogen bonds · protein-protein
- B–C · 448 Ų buried · 5 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 5PZU · PDBe 5PZU · UniProt Q2TU34
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