› 4fbp

X-ray diffraction
2.5Å resolution

CONFORMATIONAL TRANSITION OF FRUCTOSE-1,6-BISPHOSPHATASE: STRUCTURE COMPARISON BETWEEN THE AMP COMPLEX (T FORM) AND THE FRUCTOSE 6-PHOSPHATE COMPLEX (R FORM)

Released:
DOI: 10.2210/pdb4fbp/pdb
PDB entry 4fbp coloured by chain, front view.
PDB entry 4fbp coloured by chain, side view.
PDB entry 4fbp coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
Conformational transition of fructose-1,6-bisphosphatase: structure comparison between the AMP complex (T form) and the fructose 6-phosphate complex (R form).
Ke HM, Liang JY, Zhang YP, Lipscomb WN
Biochemistry 30 4412-20 (1991)
PMID: 1850623

Function and Biology Details

Reaction catalysed: 
D-fructose 1,6-bisphosphate + H(2)O = D-fructose 6-phosphate + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132778 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructose-1,6-bisphosphatase 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 335 amino acids
Theoretical weight: 36.5 KDa
Source organism: Sus scrofa
Expression system: Not provided
UniProt:
  • Canonical: P00636 (Residues: 2-336; Coverage: 99%)
Gene names: FBP, FBP1
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand AMP 4 x AMP
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 78.5Å b: 88.5Å c: 211.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.169 0.169 not available
Expression system: Not provided

Quick links

Citations

3 review citations

Folding funnels and binding mechanisms.
Ma et al. (1999)
2 more

1 mention without citation

PMFF: Development of a Physics-Based Molecular Force Field for Protein Simulation and Ligand Docking.
Hwang et al. (2020)