Structure of PDB 1fj9 Chain B Binding Site BS02
Receptor Information
>1fj9 Chain B (length=319) Species:
9823
(Sus scrofa) [
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NIVTLTRFVMEEGRKARGTGEMTQLLNSLCTAVKAISTAVRKAGIAHLWG
IAGSKKLDVLSNDLVINVLKSSFATCVLVSEEDKNAIIVEPEKRGKYVVC
FDPLDGSSNIDCLVSIGTIFGIYRKNSTDEPSEKDALQPGRNLVAAGYAL
YGSATMLVLAMVNGVNCFMLDPAIGEFILVDRDVKIKKKGSIYSINEGYA
KEFDPAITEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLVYGGIFMYPA
NKKSPKGKLRLLYECNPMAYVMEKAGGLATTGKEAVLDIVPTDIHQRAPI
ILGSPEDVTELLEIYQKHA
Ligand information
Ligand ID
ZN
InChI
InChI=1S/Zn/q+2
InChIKey
PTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Zn+2]
Formula
Zn
Name
ZINC ION
ChEMBL
CHEMBL1236970
DrugBank
DB14532
ZINC
PDB chain
1fj9 Chain B Residue 413 [
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Receptor-Ligand Complex Structure
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PDB
1fj9
Tryptophan fluorescence reveals the conformational state of a dynamic loop in recombinant porcine fructose-1,6-bisphosphatase.
Resolution
2.5 Å
Binding residue
(original residue number in PDB)
D118 D121 E280
Binding residue
(residue number reindexed from 1)
D102 D105 E264
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
D74 E97 E98 D118 L120 D121 E280
Catalytic site (residue number reindexed from 1)
D58 E81 E82 D102 L104 D105 E264
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:1fj9
,
PDBe:1fj9
,
PDBj:1fj9
PDBsum
1fj9
PubMed
10998248
UniProt
P00636
|F16P1_PIG Fructose-1,6-bisphosphatase 1 (Gene Name=FBP1)
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