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2QVR

E. coli Fructose-1,6-bisphosphatase: Citrate, Fru-2,6-P2, and Mg2+ bound

Summary for 2QVR
Entry DOI10.2210/pdb2qvr/pdb
Related2GQ1 2OWZ 2OX3 2Q8M 2QVU 2QVV
DescriptorFructose-1,6-bisphosphatase, 2,6-di-O-phosphono-beta-D-fructofuranose, MAGNESIUM ION, ... (5 entities in total)
Functional Keywordstetramer, sugar phosphatase fold, carbohydrate metabolism, cytoplasm, hydrolase, magnesium
Biological sourceEscherichia coli
Total number of polymer chains1
Total formula weight37717.78
Authors
Hines, J.K.,Fromm, H.J.,Honzatko, R.B. (deposition date: 2007-08-08, release date: 2007-10-23, Last modification date: 2023-11-15)
Primary citationHines, J.K.,Chen, X.,Nix, J.C.,Fromm, H.J.,Honzatko, R.B.
Structures of Mammalian and Bacterial Fructose-1,6-bisphosphatase Reveal the Basis for Synergism in AMP/Fructose 2,6-Bisphosphate Inhibition.
J.Biol.Chem., 282:36121-36131, 2007
Cited by
PubMed: 17933867
DOI: 10.1074/jbc.M707302200
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.18 Å)
Structure validation

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