Structure of PDB 1q9d Chain B Binding Site BS01

Receptor Information
>1q9d Chain B (length=328) Species: 9823 (Sus scrofa) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TNIVTLTRFVMEEGRKARGTGEMTQLLNSLCTAVKAISTAVRKAGIAHLY
GIAGSTNVTGDQVKKLDVLSNDLVINVLKSSFATCVLVSEEDKNAIIVEP
EKRGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKNSTDEPSEKDALQPGR
NLVAAGYALYGSATMLVLAMVNGVNCFMLDPAIGEFILVDRDVKIKKKGS
IYSINEGYAKEFDPAITEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLV
YGGIFMYPANKKSPKGKLRLLYECNPMAYVMEKAGGLATTGKEAVLDIVP
TDIHQRAPIILGSPEDVTELLEIYQKHA
Ligand information
Ligand IDOI1
InChIInChI=1S/C32H35N3O5/c1-2-5-27(30(38)33-17-16-21-8-12-25(36)13-9-21)35-29(18-22-10-14-26(37)15-11-22)31(39)34-20-24-7-4-3-6-23(24)19-28(34)32(35)40/h3-4,6-15,27-29H,2,5,16-20H2,1H3,(H3,33,36,37,38)/t27-,28-,29-/m0/s1
InChIKeyGSRXSLSGKZHATI-AWCRTANDSA-N
SMILES
SoftwareSMILES
CACTVS 3.341CCC[C@@H](C(=O)NCCc1ccc(O)cc1)[N+]2=C([O-])[C@@H]3Cc4ccccc4CN3C(=O)[C@@H]2Cc5ccc(O)cc5
OpenEye OEToolkits 1.5.0CCC[C@@H](C(=O)NCCc1ccc(cc1)O)[N+]2=C([C@@H]3Cc4ccccc4CN3C(=O)[C@@H]2Cc5ccc(cc5)O)[O-]
CACTVS 3.341CCC[CH](C(=O)NCCc1ccc(O)cc1)[N+]2=C([O-])[CH]3Cc4ccccc4CN3C(=O)[CH]2Cc5ccc(O)cc5
OpenEye OEToolkits 1.5.0CCCC(C(=O)NCCc1ccc(cc1)O)[N+]2=C(C3Cc4ccccc4CN3C(=O)C2Cc5ccc(cc5)O)[O-]
ACDLabs 10.04O=C(NCCc1ccc(O)cc1)C([N+]2=C([O-])C5N(C(=O)C2Cc3ccc(O)cc3)Cc4c(cccc4)C5)CCC
FormulaC32 H35 N3 O5
Name3-(4-HYDROXYBENZYL)-2-[1-({[2-(4-HYDROXYPHENYL)ETHYL]AMINO}CARBONYL)BUTYL]-4-OXO-3,6,11,11A-TETRAHYDRO-4H-PYRAZINO[1,2-B]ISOQUINOLIN-2-IUM-1-OLATE
ChEMBL
DrugBank
ZINC
PDB chain1q9d Chain A Residue 416 [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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PDB1q9d Inhibition of fructose-1,6-bisphosphatase by a new class of allosteric effectors
Resolution2.35 Å
Binding residue
(original residue number in PDB)		G52 H55
Binding residue
(residue number reindexed from 1)		G45 H48
Annotation score1
Binding affinityMOAD: ic50=1.87uM
PDBbind-CN: -logKd/Ki=4.60,Kd=25uM
Enzymatic activity
Catalytic site (original residue number in PDB) D68 D74 E97 E98 D118 L120 D121 E280
Catalytic site (residue number reindexed from 1) D61 D67 E90 E91 D111 L113 D114 E273
Enzyme Commision number 3.1.3.11: fructose-bisphosphatase.
Gene Ontology
Molecular Function
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
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:0006111 regulation of gluconeogenesis
GO:0016311 dephosphorylation
GO:0030308 negative regulation of cell growth
GO:0030388 fructose 1,6-bisphosphate metabolic process
GO:0045820 negative regulation of glycolytic process
GO:0046580 negative regulation of Ras protein signal transduction
GO:0071286 cellular response to magnesium ion
GO:0071466 cellular response to xenobiotic stimulus
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1q9d, PDBe:1q9d, PDBj:1q9d
PDBsum1q9d
PubMed14530289
UniProtP00636|F16P1_PIG Fructose-1,6-bisphosphatase 1 (Gene Name=FBP1)

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