Structure of PDB 1nuz Chain A Binding Site BS06

Receptor Information
>1nuz Chain A (length=329) Species: 9823 (Sus scrofa) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DTNIVTLTRFVMEEGRKARGTGEMTQLLNSLCTAVKAISTAVRKAGIAHL
YGIAGSTNVTGDQVKKLDVLSNDLVINVLKSSFATCVLVSEEDKNAIIVE
PEKRGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKNSTDEPSEKDALQPG
RNLVAAGYALYGSATMLVLAMVNGVNCFMLDPAIGEFILVDRDVKIKKKG
SIYSINEGYAKEFDPAITEYIQRKKFPPDNSAPYGARYVGSMVADVHRTL
VYGGIFMYPANKKSPKGKLRLLYECNPMAYVMEKAGGLATTGKEAVLDIV
PTDIHQRAPIILGSPEDVTELLEIYQKHA
Ligand information
Ligand IDPO4
InChIInChI=1S/H3O4P/c1-5(2,3)4/h(H3,1,2,3,4)/p-3
InChIKeyNBIIXXVUZAFLBC-UHFFFAOYSA-K
SMILES
SoftwareSMILES
CACTVS 3.341[O-][P]([O-])([O-])=O
ACDLabs 10.04[O-]P([O-])([O-])=O
OpenEye OEToolkits 1.5.0[O-]P(=O)([O-])[O-]
FormulaO4 P
NamePHOSPHATE ION
ChEMBL
DrugBankDB14523
ZINC
PDB chain1nuz Chain A Residue 2340 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1nuz Interaction of Tl+ with product complexes of fructose-1,6-bisphosphatase
Resolution1.9 Å
Binding residue
(original residue number in PDB)		E1097 D1118 L1120 D1121 G1122 S1123 R1276
Binding residue
(residue number reindexed from 1)		E91 D112 L114 D115 G116 S117 R270
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) D1068 D1074 E1097 E1098 D1118 L1120 D1121 E1280
Catalytic site (residue number reindexed from 1) D62 D68 E91 E92 D112 L114 D115 E274
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:1nuz, PDBe:1nuz, PDBj:1nuz
PDBsum1nuz
PubMed12595529
UniProtP00636|F16P1_PIG Fructose-1,6-bisphosphatase 1 (Gene Name=FBP1)

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