MolNFT v1 · #92557 · protein
Crystal structure of AMP complexes of porcine liver fructose-1,6- bisphosphatase mutant A54L with 1,2-ethanediol as cryo-protectant
4GBV · Fructose-1,6-bisphosphatase 1: “Crystal structure of AMP complexes of porcine liver fructose-1,6- bisphosphatase mutant A54L with…”. X-ray diffraction, 4 ligands (F6P, AMP, MN), 2 pockets (best druggability 0.54). MolNFT v1 #92557…
- PDB
- 4GBV
- Type
- protein
- Length
- 326 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fructose-1,6-bisphosphatase 1
- EC
- 3.1.3.11
- UniProt
- P00636
- Ligands
- F6P, AMP, MN, PO4
- Pockets
- 2 · best druggability 0.54
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fructose-1,6-bisphosphatase 1 (EC 3.1.3.11) | protein | 326 | 35% helix, 28% strand | P00636 |
Ligands and binding sites
- F6P · 6-O-phosphono-beta-D-fructofuranose · ligand · chains A
- AMP · Adenosine monophosphate · ligand · chains A
- MN · Manganese (II) ion · metal · 2 copies · chains A
- PO4 · Phosphate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 119 | 0.54 | 0.83 | 25 | F6P, PO4, MN |
| 2 | 171 | 0.51 | 0.78 | 31 | AMP |
Compared structures
- 4GBV · Crystal Structure of AMP complexes of Porcine Liver Fructose-1,6-bisphosphatase Mutant… · the same entry in another collection · chain A against A, TM-score 1.00
- P00636 · AlphaFold monomer V2.0 prediction for fructose-1,6-bisphosphatase 1 (P00636) · a predicted model of the same protein · chain A against A, TM-score 1.00
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 P00636
- Elsewhere: RCSB PDB 4GBV · PDBe 4GBV · UniProt P00636
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