Structure of PDB 5ldz Chain D Binding Site BS01

Receptor Information
>5ldz Chain D (length=313) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PFDTDVNTLTRFVMEEGGTGELTQLLNSLCTAVKAISSAVRKAGIAHLKK
LDVLSNDLVMNMLKSSFATCVLVSEEDKHAIIVEPEKRGKYVVCFDPLDG
SSNIDCLVSVGTIFGIYRKKSTDEPSEKDALQPGRNLVAAGYALYGSATM
LVLAMDCGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYARDFDPA
VTEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLVYGGIFLYPANKKSPN
GKLRLLYECNPMAYVMEKAGGMATTGKEAVLDVIPTDIHQRAPVILGSPD
DVLEFLKVYEKHS
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain5ldz Chain D Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5ldz Quadruple space-group ambiguity owing to rotational and translational noncrystallographic symmetry in human liver fructose-1,6-bisphosphatase.
Resolution2.2 Å
Binding residue
(original residue number in PDB)		E98 D119 D122 E281
Binding residue
(residue number reindexed from 1)		E75 D96 D99 E258
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) D75 E98 E99 D119 L121 D122 E281
Catalytic site (residue number reindexed from 1) D52 E75 E76 D96 L98 D99 E258
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
View graph for
Cellular Component
External links
PDB RCSB:5ldz, PDBe:5ldz, PDBj:5ldz
PDBsum5ldz
PubMed27841754
UniProtP09467|F16P1_HUMAN Fructose-1,6-bisphosphatase 1 (Gene Name=FBP1)

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