› 1fbc

X-ray diffraction
2.6Å resolution

CRYSTALLOGRAPHIC STUDIES OF THE CATALYTIC MECHANISM OF THE NEUTRAL FORM OF FRUCTOSE-1,6-BISPHOSPHATASE

Released:
DOI: 10.2210/pdb1fbc/pdb
PDB entry 1fbc coloured by chain, front view.
PDB entry 1fbc coloured by chain, side view.
PDB entry 1fbc coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
Crystallographic studies of the catalytic mechanism of the neutral form of fructose-1,6-bisphosphatase.
Zhang Y, Liang JY, Huang S, Ke H, Lipscomb WN
Biochemistry 32 1844-57 (1993)
PMID: 8382525

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
Molecule details ›
Chains: A, B
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

2 bound ligands:
Ligand MG 2 x MG
Ligand AHG 2 x AHG
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3221
Unit cell:
a: 131.4Å b: 131.4Å c: 68.9Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.185 0.185 not available
Expression system: Not provided

Quick links

Citations

6 review citations

Zinc enzymes.
Coleman JE. (1998)
5 more

2 mentions without citation

Optimal clustering for detecting near-native conformations in protein docking.
Kozakov et al. (2005)
1 more