Research workbench
Structure of yeast FBP1 (fructose-1,6-bisphosphatase 1)
Analyse Structure of yeast FBP1 (fructose-1,6-bisphosphatase 1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7NS5
- Type
- protein
- Length
- 1,214 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fructose-1,6-bisphosphatase
- EC
- 3.1.3.11
- UniProt
- P09201
- Ligands
- MG, PO4
- Pockets
- 17 · best druggability 0.85
Structure
x-ray diffraction · 4 distinct chains · 39% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fructose-1,6-bisphosphatase (EC 3.1.3.11) | protein | 319 | 39% helix, 24% strand | P09201 |
| D | Fructose-1,6-bisphosphatase (EC 3.1.3.11) | protein | 290 | 38% helix, 26% strand | P09201 |
| B | Fructose-1,6-bisphosphatase (EC 3.1.3.11) | protein | 312 | 39% helix, 24% strand | P09201 |
| C | Fructose-1,6-bisphosphatase (EC 3.1.3.11) | protein | 293 | 39% helix, 28% strand | P09201 |
Ligands and binding sites
- MG · Magnesium ion · metal · 8 copies · chains A, D, B, C
- PO4 · Phosphate ion · ion · 4 copies · chains A, D, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
17 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 313 | 0.85 | 0.96 | 43 | empty |
| 2 | 91 | 0.76 | 0.97 | 22 | empty |
| 3 | 235 | 0.74 | 0.88 | 26 | empty |
| 4 | 224 | 0.73 | 0.88 | 26 | empty |
| 5 | 57 | 0.60 | 0.92 | 18 | empty |
Interfaces
6 interfaces between chains.
- B–C · 2395 Ų buried · 34 hydrogen bonds · protein-protein
- A–D · 2386 Ų buried · 35 hydrogen bonds · protein-protein
- A–B · 1209 Ų buried · 18 hydrogen bonds · protein-protein
- D–C · 975 Ų buried · 10 hydrogen bonds · protein-protein
- D–B · 433 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
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 P09201
- Elsewhere: RCSB PDB 7NS5 · PDBe 7NS5 · UniProt P09201
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