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EBI PDBe PDBeView

PDBe Entry: 1fbc view

CRYSTALLOGRAPHIC STUDIES OF THE CATALYTIC MECHANISM OF THE NEUTRAL FORM OF FRUCTOSE-1,6-BISPHOSPHATASE
Summary
Header HYDROLASE(PHOSPHORIC MONOESTER)search
Method X-RAY DIFFRACTION
Experiment Resolution: 2.6 Å, R-factor: 18.5%, Spacegroup: P 32 2 1
Released 31/10/1993, deposition: 14/10/1992, last revision: 24/02/2009
Authors Zhang, Y.search; Liang, J.-Y.search; Huang, S.search; Ke, H.search; Lipscomb, W.N.search
Primary citation Crystallographic studies of the catalytic mechanism of the neutral form of fructose-1,6-bisphosphatase.
BIOCHEMISTRYsearch vol:32, pag:1844-1857 (1993) [PubMed ID 8382525 ]search
Keywords HYDROLASE(PHOSPHORIC MONOESTER)search
EC 3.1.3.11 ExPASy BRENDA search (A B)
Organism Sus scrofa(pig) 9823search(A B)
UniProt Fructose-1,6-bisphosphatase 1 (EC 3.1.3.11) (FBPase 1) (D-fructose-1,6-bisphosphate 1-phosphohydrolase 1) P00636search (A B)
Solvent A, B
Polymers
Id Name Type UniProt Residues Observed
A, B FRUCTOSE 1,6-BISPHOSPHATASE Protein P00636 (F16P1_PIG)search
 335 94%
Heterogens
Id Name Ligands
A, B MAGNESIUM ION MG search
A, B 2,5-ANHYDROGLUCITOL-1,6-BIPHOSPHATE AHG search
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