Structure of PDB 2qvr Chain A

Receptor sequence
>2qvrA (length=332) Species: 562 (Escherichia coli) [Search protein sequence]
MKTLGEFIVEKQHEFSHATGELTALLSAIKLGAKIIHRDINKAGLVDILG
ASGAENVQGEVQQKLDLFANEKLKAALKARDIVAGIASEEEDEIVVFEGC
EHAKYVVLMDPLDGSSNIDVNVSVGTIFSIYRRVTPVGTPVTEEDFLQPG
NKQVAAGYVVYGSSTMLVYTTGCGVHAFTYDPSLGVFCLCQERMRFPEKG
KTYSINEGNYIKFPNGVKKYIKFCQEEDKSTNRPYTSRYIGSLVADFHRN
LLKGGIYLYPSTASHPDGKLRLLYECNPMAFLAEQAGGKASDGKERILDI
IPETLHQRRSFFVGNDHMVEDVERFIREFPDA
3D structure
PDB2qvr Structures of Mammalian and Bacterial Fructose-1,6-bisphosphatase Reveal the Basis for Synergism in AMP/Fructose 2,6-Bisphosphate Inhibition.
ChainA
Resolution2.18 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E60 D66 E89 E90 D110 L112 D113 E275
Catalytic site (residue number reindexed from 1) E60 D66 E89 E90 D110 L112 D113 E275
Enzyme Commision number 3.1.3.11: fructose-bisphosphatase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 FDP A D113 G114 S115 S116 N206 Y239 G241 L243 Y257 Y259 K269 D113 G114 S115 S116 N206 Y239 G241 L243 Y257 Y259 K269
BS02 MG A D110 D113 E275 D110 D113 E275
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0000287 magnesium ion binding
GO:0016787 hydrolase activity
GO:0016791 phosphatase activity
GO:0042132 fructose 1,6-bisphosphate 1-phosphatase activity
GO:0042578 phosphoric ester hydrolase activity
GO:0042802 identical protein binding
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0005986 sucrose biosynthetic process
GO:0006000 fructose metabolic process
GO:0006002 fructose 6-phosphate metabolic process
GO:0006094 gluconeogenesis
GO:0030388 fructose 1,6-bisphosphate metabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0032991 protein-containing complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2qvr, PDBe:2qvr, PDBj:2qvr
PDBsum2qvr
PubMed17933867
UniProtP0A993|F16PA_ECOLI Fructose-1,6-bisphosphatase class 1 (Gene Name=fbp)

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