Structure of PDB 2q8m Chain A Binding Site BS05

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 IDAMP
InChIInChI=1S/C10H14N5O7P/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(22-10)1-21-23(18,19)20/h2-4,6-7,10,16-17H,1H2,(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
InChIKeyUDMBCSSLTHHNCD-KQYNXXCUSA-N
SMILES
SoftwareSMILES
CACTVS 3.370Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(O)=O)[CH](O)[CH]3O
CACTVS 3.370Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P](O)(O)=O)[C@@H](O)[C@H]3O
OpenEye OEToolkits 1.7.6c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)COP(=O)(O)O)O)O)N
ACDLabs 12.01O=P(O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
OpenEye OEToolkits 1.7.6c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)O)O)O)N
FormulaC10 H14 N5 O7 P
NameADENOSINE MONOPHOSPHATE
ChEMBLCHEMBL752
DrugBankDB00131
ZINCZINC000003860156
PDB chain2q8m Chain A Residue 341 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB2q8m 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.
Resolution2.05 Å
Binding residue
(original residue number in PDB)		I8 Q12 F15 A18 T19 G20 E21 L22 K104 Y105
Binding residue
(residue number reindexed from 1)		I8 Q12 F15 A18 T19 G20 E21 L22 K82 Y83
Annotation score1
Binding affinityMOAD: Ki=94uM
PDBbind-CN: -logKd/Ki=4.03,Ki=94uM
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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2q8m, PDBe:2q8m, PDBj:2q8m
PDBsum2q8m
PubMed17567577
UniProtP0A993|F16PA_ECOLI Fructose-1,6-bisphosphatase class 1 (Gene Name=fbp)

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