Het-PDB Navi2 (PDB: 1FSA)

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Ligands
Code	Name	Link
AMP	Adenosine monophosphate	PoSSuM
MN	Manganese (II) ion	PoSSuM
F6P	6-O-phosphono-beta-D-fructofuranose	PoSSuM

Non-standard Residues
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Glycosylation
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Download interaction data: 1FSA

Code :

1FSA PDBj RCSB PDB PDBe

Header :

HYDROLASE

Title :

THE T-STATE STRUCTURE OF LYS 42 TO ALA MUTANT OF THE PIG KIDNEY FRUCTOSE 1,6-BISPHOSPHATASE EXPRESSED IN E. COLI

Release Data :

1997-09-04

Compound :

mol_id	molecule	chains
1	FRUCTOSE 1,6-BISPHOSPHATASE	A,B
	ec: 3.1.3.11 mutation: K42A

Source :

mol_id	organism_scientific	organism_common	expression_system
1	Sus scrofa (taxid:9823)	Pig	Escherichia coli (taxid:562)
	organ: KIDNEY gene: FBP expression_system_strain: EK1601 expression_system_plasmid: PEK292 expression_system_gene: FBP

Authors :

Lu, G., Stec, B., Giroux, E., Kantrowitz, E.R.

Keywords :

LYASE, FRUCTOSE 1, 6-BISPHOSPHATASE, HYDROLASE, CARBOHYDRATE METABOLISM, GLUCONEOGENESIS, ACETYLATION PHOSPHORYLATION

Exp. method :

X-RAY DIFFRACTION ( 2.3 Å )

Citation :

Evidence for an active T-state pig kidney fructose 1,6-bisphosphatase: interface residue Lys-42 is important for allosteric inhibition and AMP cooperativity.

Lu, G.,Stec, B.,Giroux, E.L. et al.
(1996) Protein Sci. 5 : 2333 - 2342

PubMed: 8931152

Crystal Structures of the Active Site Mutant (Arg-243-->Ala) in the T and R Allosteric States of Pig Kidney Fructose-1,6-Bisphosphatase Expressed in Escherichia Coli

Stec, B.,Abraham, R.,Giroux, E. et al.
(1996) Protein Sci. 5 : 1541

Crystal Structure of Fructose-1,6-Bisphosphatase Complexed with Fructose 2,6-Bisphosphate, AMP, and Zn2+ at 2.0-A Resolution: Aspects of Synergism between Inhibitors

Xue, Y.,Huang, S.,Liang, J.Y. et al.
(1994) Proc.Natl.Acad.Sci.USA 91 : 12482

Crystal Structure of the Neutral Form of Fructose-1,6-Bisphosphatase Complexed with the Product Fructose 6-Phosphate at 2.1-A Resolution

Ke, H.,Zhang, Y.,Liang, J.Y. et al.
(1991) Proc.Natl.Acad.Sci.USA 88 : 2989

Chain :

A, B

UniProt :

P00636 (F16P1_PIG)

Reaction:	EC:	Evidence:
Reaction:	Physiological Direction:	Evidence:
beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6- phosphate + phosphate	3.1.3.11	PubMed:15767255, PubMed:1313579
	-	PubMed:15767255, PubMed:1313579

PDB ID: 1FSA

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Structure summary

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