MolNFT v1 · #174890 · protein
Crystal structure of human liver fructose-1,6-bisphoaphatase complex with MG2+ and AMP
7C9Q · Fructose-1,6-bisphosphatase 1: “Crystal structure of human liver fructose-1,6-bisphoaphatase complex with MG2+ and AMP”. X-ray diffraction, 2 ligands (AMP, MG), 20 pockets (best druggability 0.88). MolNFT v1 #174890 on GenesisL1: 3D…
- PDB
- 7C9Q
- Type
- protein
- Length
- 1,295 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
- P09467
- Ligands
- AMP, MG
- Pockets
- 20 · best druggability 0.88
Structure
x-ray diffraction · 4 distinct chains · 38% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fructose-1,6-bisphosphatase 1 (EC 3.1.3.11) | protein | 327 | 37% helix, 24% strand | P09467 |
| C | Fructose-1,6-bisphosphatase 1 (EC 3.1.3.11) | protein | 319 | 39% helix, 24% strand | P09467 |
| D | Fructose-1,6-bisphosphatase 1 (EC 3.1.3.11) | protein | 326 | 38% helix, 23% strand | P09467 |
| B | Fructose-1,6-bisphosphatase 1 (EC 3.1.3.11) | protein | 323 | 37% helix, 22% strand | P09467 |
Ligands and binding sites
- AMP · Adenosine monophosphate · ligand · 4 copies · chains A, C, D, B
- MG · Magnesium ion · metal · 4 copies · chains A, C, D, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1141 | 0.88 | 0.89 | 111 | empty |
| 2 | 53 | 0.71 | 0.99 | 28 | empty |
| 3 | 92 | 0.62 | 0.89 | 31 | empty |
| 4 | 213 | 0.59 | 0.81 | 49 | empty |
| 5 | 91 | 0.55 | 0.85 | 20 | empty |
Interfaces
6 interfaces between chains.
- A–B · 2399 Ų buried · 39 hydrogen bonds · protein-protein
- C–D · 2329 Ų buried · 29 hydrogen bonds · protein-protein
- A–C · 1277 Ų buried · 27 hydrogen bonds · protein-protein
- D–B · 1243 Ų buried · 29 hydrogen bonds · protein-protein
- A–D · 545 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 7C9Q · Crystal structure of Human liver fructose-1,6-bisphoaphatase complex with Mg2+ and AMP · the same entry in another collection · chain B against B, 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 C against A, TM-score 0.96
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 7C9Q · PDBe 7C9Q · UniProt P09467
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