Research workbench
Crystal structure of AMP complexes of porcine liver fructose-1,6- bisphosphatase with blocked subunit pair rotation
Analyse Crystal structure of AMP complexes of porcine liver fructose-1,6… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4GWY
- 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, MG, PO4
- Pockets
- 3 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fructose-1,6-bisphosphatase 1 (EC 3.1.3.11) | protein | 326 | 35% helix, 24% strand | P00636 |
Ligands and binding sites
- F6P · 6-O-phosphono-beta-D-fructofuranose · ligand · chains A
- AMP · Adenosine monophosphate · ligand · chains A
- MG · Magnesium ion · metal · 3 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
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 53 | 0.71 | 0.97 | 25 | empty |
| 2 | 125 | 0.54 | 0.82 | 21 | F6P, PO4, MG |
| 3 | 128 | 0.48 | 0.79 | 28 | AMP |
Compared structures
- 4GWY · Crystal Structure of AMP Complexes of Porcine Liver Fructose-1,6-bisphosphatase with… · 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 4GWY · PDBe 4GWY · UniProt P00636
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