MolNFT v1 · #6990 · protein
Fructose-1,6-BISPHOSPHATASE(D-fructose-1,6-bisphosphate, 1- phosphohydrolase) (E.C.3.1.3.11) complexed with the allosteric inhibitor AMP
1FTA: “Fructose-1,6-BISPHOSPHATASE(D-fructose-1,6-bisphosphate, 1- phosphohydrolase) (E.C.3.1.3.11) complexed with…”. X-ray diffraction, 1 ligand (AMP), 18 pockets (best druggability 0.84). MolNFT v1 #6990 on GenesisL1: 3D structure…
- PDB
- 1FTA
- 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
- EC
- 3.1.3.11
- UniProt
- P09467
- Ligands
- AMP
- Pockets
- 18 · best druggability 0.84
Structure
x-ray diffraction · 3 distinct chains · 38% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fructose-1,6-bisphosphatase (EC 3.1.3.11) | protein | 319 | 38% helix, 25% strand | P09467 |
| B, C | Fructose-1,6-bisphosphatase (EC 3.1.3.11) | protein | 317 | 39% helix, 26% strand | P09467 |
| D | Fructose-1,6-bisphosphatase (EC 3.1.3.11) | protein | 318 | 37% helix, 25% strand | P09467 |
Ligands and binding sites
- AMP · Adenosine monophosphate · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
18 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1062 | 0.84 | 0.85 | 112 | empty |
| 2 | 68 | 0.74 | 0.98 | 28 | empty |
| 3 | 282 | 0.60 | 0.78 | 43 | AMP |
| 4 | 289 | 0.58 | 0.77 | 44 | AMP |
| 5 | 219 | 0.55 | 0.78 | 39 | empty |
Interfaces
6 interfaces between chains.
- C–D · 2343 Ų buried · 28 hydrogen bonds · protein-protein
- A–B · 2289 Ų buried · 27 hydrogen bonds · protein-protein
- A–C · 1259 Ų buried · 22 hydrogen bonds · protein-protein
- B–D · 1159 Ų buried · 18 hydrogen bonds · protein-protein
- B–C · 434 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 1FTA · Fructose-1,6-BISPHOSPHATASE(D-fructose-1,6-bisphosphate, 1-phosphohydrolase)… · the same entry in another collection · chain D against D, TM-score 1.00
- P09467 · AlphaFold monomer V2.0 prediction for fructose-1,6-bisphosphatase 1 (P09467) · a predicted model of the same protein · chain B against A, TM-score 0.97
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 P09467
- Elsewhere: RCSB PDB 1FTA · PDBe 1FTA · UniProt P09467
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