Structure of PDB 2q8m Chain A Binding Site BS02

Receptor Information

>2q8m Chain A (length=310) Species: 621 (Shigella boydii) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

MKTLGEFIVEKQHEFSHATGELTALLSAIKLGAKIIHRDINKAGLFANEK
LKAALKARDIVAGIASEEEDEIVVFEGCEHAKYVVLMDPLDGSSNIDVNV
SVGTIFSIYRRVTPVGTPVTEEDFLQPGNKQVAAGYVVYGSSTMLVYTTG
CGVHAFTYDPSLGVFCLCQERMRFPEKGKTYSINEGNYIKFPNGVKKYIK
FCQEEDKSTNRPYTSRYIGSLVADFHRNLLKGGIYLYPSTASHPDGKLRL
LYECNPMAFLAEQAGGKASDGKERILDIIPETLHQRRSFFVGNDHMVEDV
ERFIREFPDA

Ligand information

Ligand ID

FBP

InChI

InChI=1S/C6H14O12P2/c7-4-3(1-16-19(10,11)12)18-6(9,5(4)8)2-17-20(13,14)15/h3-5,7-9H,1-2H2,(H2,10,11,12)(H2,13,14,15)/t3-,4-,5+,6-/m1/s1

InChIKey

RNBGYGVWRKECFJ-ARQDHWQXSA-N

SMILES

Software	SMILES
CACTVS 3.341	O[C@H]1[C@H](O)[C@@](O)(CO[P](O)(O)=O)O[C@@H]1CO[P](O)(O)=O
CACTVS 3.341	O[CH]1[CH](O)[C](O)(CO[P](O)(O)=O)O[CH]1CO[P](O)(O)=O
ACDLabs 10.04	O=P(O)(O)OCC1OC(O)(COP(=O)(O)O)C(O)C1O
OpenEye OEToolkits 1.5.0	C(C1C(C(C(O1)(COP(=O)(O)O)O)O)O)OP(=O)(O)O
OpenEye OEToolkits 1.5.0	C([C@@H]1[C@H]([C@@H]([C@](O1)(COP(=O)(O)O)O)O)O)OP(=O)(O)O

Formula

C6 H14 O12 P2

Name

1,6-di-O-phosphono-beta-D-fructofuranose;
BETA-FRUCTOSE-1,6-DIPHOSPHATE;
FRUCTOSE-1,6-BISPHOSPHATE;
1,6-di-O-phosphono-beta-D-fructose;
1,6-di-O-phosphono-D-fructose;
1,6-di-O-phosphono-fructose

PDB chain

2q8m Chain A Residue 344 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

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Structure summary

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PDB	2q8m Structure of Inhibited Fructose-1,6-bisphosphatase from Escherichia coli: DISTINCT ALLOSTERIC INHIBITION SITES FOR AMP AND GLUCOSE 6-PHOSPHATE AND THE CHARACTERIZATION OF A GLUCONEOGENIC SWITCH.
Resolution	2.05 Å
Binding residue (original residue number in PDB)	D110 D113 G114 N206 Y239 L243 Y257 Y259 K269 E275
Binding residue (residue number reindexed from 1)	D88 D91 G92 N184 Y217 L221 Y235 Y237 K247 E253
Annotation score	5
Binding affinity	MOAD: ic50=6uM

Enzymatic activity

Catalytic site (original residue number in PDB)	E89 E90 D110 L112 D113 E275
Catalytic site (residue number reindexed from 1)	E67 E68 D88 L90 D91 E253
Enzyme Commision number	3.1.3.11: fructose-bisphosphatase.

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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Cellular Component

External links

PDB	RCSB:2q8m, PDBe:2q8m, PDBj:2q8m
PDBsum	2q8m
PubMed	17567577
UniProt	P0A993\|F16PA_ECOLI Fructose-1,6-bisphosphatase class 1 (Gene Name=fbp)

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