Structure of PDB 2y5l Chain C Binding Site BS01

Receptor Information
>2y5l Chain C (length=317) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DVNTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAVRKAGIAHLYG
IAGKLDVLSNDLVMNMLKSSFATCVLVSEEDKHAIIVEPEKRGKYVVCFD
PLDGSSNIDCLVSVGTIFGIYRKKSTDEPSEKDALQPGRNLVAAGYALYG
SATMLVLAMDCGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYAKD
FDPAVTEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLVYGGIFLYPANK
KSPNGKLRLLYECNPMAYVMEKAGGMATTGKEAVLDVIPTDIHQRAPVIL
GSPDDVLEFLKVYEKHS
Ligand information
Ligand IDRO8
InChIInChI=1S/C10H7BrClN3O3S2/c11-8-5-13-10(19-8)14-9(16)15-20(17,18)7-3-1-2-6(12)4-7/h1-5H,(H2,13,14,15,16)
InChIKeyVRHXEPNJEQXSSS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.352Clc1cccc(c1)[S](=O)(=O)NC(=O)N=C2NC=C(Br)S2
OpenEye OEToolkits 1.6.1c1cc(cc(c1)Cl)S(=O)(=O)NC(=O)N=C2NC=C(S2)Br
OpenEye OEToolkits 1.6.1c1cc(cc(c1)Cl)S(=O)(=O)NC(=O)/N=C\2/NC=C(S2)Br
ACDLabs 12.01BrC=2S/C(=N\C(=O)NS(=O)(=O)c1cccc(Cl)c1)NC=2
FormulaC10 H7 Br Cl N3 O3 S2
NameN-{[(2Z)-5-bromo-1,3-thiazol-2(3H)-ylidene]carbamoyl}-3-chlorobenzenesulfonamide;
RO5062408
ChEMBLCHEMBL595149
DrugBank
ZINCZINC000045348530
PDB chain2y5l Chain C Residue 1000 [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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PDB2y5l Orally Active Aminopyridines as Inhibitors of Tetrameric Fructose-1,6-Bisphosphatase.
Resolution2.2 Å
Binding residue
(original residue number in PDB)		V17 M18 G21 R22 G26 G28 L30 T31
Binding residue
(residue number reindexed from 1)		V9 M10 G13 R14 G18 G20 L22 T23
Annotation score1
Binding affinityMOAD: ic50=0.33uM
PDBbind-CN: -logKd/Ki=6.48,IC50=0.33uM
Enzymatic activity
Catalytic site (original residue number in PDB) D74 E97 E98 D118 L120 D121 E280
Catalytic site (residue number reindexed from 1) D56 E79 E80 D100 L102 D103 E262
Enzyme Commision number 3.1.3.11: fructose-bisphosphatase.
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0016208 AMP 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
GO:0048029 monosaccharide binding
GO:0061629 RNA polymerase II-specific DNA-binding transcription factor binding
Biological Process
GO:0000122 negative regulation of transcription by RNA polymerase II
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:0006111 regulation of gluconeogenesis
GO:0016311 dephosphorylation
GO:0030308 negative regulation of cell growth
GO:0030388 fructose 1,6-bisphosphate metabolic process
GO:0031667 response to nutrient levels
GO:0032869 cellular response to insulin stimulus
GO:0045820 negative regulation of glycolytic process
GO:0046580 negative regulation of Ras protein signal transduction
GO:0071286 cellular response to magnesium ion
GO:0071320 cellular response to cAMP
GO:0071466 cellular response to xenobiotic stimulus
GO:0071475 cellular hyperosmotic salinity response
GO:0071477 cellular hypotonic salinity response
GO:0097403 cellular response to raffinose
GO:1904628 cellular response to phorbol 13-acetate 12-myristate
Cellular Component
GO:0005615 extracellular space
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0070062 extracellular exosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2y5l, PDBe:2y5l, PDBj:2y5l
PDBsum2y5l
PubMed21550236
UniProtP09467|F16P1_HUMAN Fructose-1,6-bisphosphatase 1 (Gene Name=FBP1)

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