Structure of PDB 1fpf Chain B

Receptor sequence
>1fpfB (length=317) Species: 9823 (Sus scrofa) [Search protein sequence]
NIVTLTRFVMEQGRKARGTGEMTQLLNSLCTAVKAISTAVRKAGIAHLYG
IAGKLDVLSNDLVINVLKSSFATCVLVTEEDKNAIIVEPEKRGKYVVCFD
PLDGSSNIDCLVSIGTIFGIYRKNSTDEPSEKDALQPGRNLVAAGYALYG
SATMLVLAMVNGVNCFMLDPAIGEFILVDRNVKIKKKGSIYSINEGYAKE
FDPAITEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLVYGGIFMYPANK
KSPKGKLRLLYECNPMAYVMEKAGGLATTGKEAVLDIVPTDIHQRAPIIL
GSPEDVTELLEIYQKHA
3D structure
PDB1fpf Structural aspects of the allosteric inhibition of fructose-1,6-bisphosphatase by AMP: the binding of both the substrate analogue 2,5-anhydro-D-glucitol 1,6-bisphosphate and catalytic metal ions monitored by X-ray crystallography.
ChainB
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 MN B E97 D118 D121 E280 E79 D100 D103 E262
BS02 MN B E97 E98 D118 P119 L120 E79 E80 D100 P101 L102
BS03 AHG B D121 G122 Y215 Y244 M248 Y264 K274 D103 G104 Y197 Y226 M230 Y246 K256
BS04 AMP B Q20 G21 G26 T27 E29 M30 K112 Y113 R140 M177 Q12 G13 G18 T19 E21 M22 K94 Y95 R122 M159 BindingDB: IC50=1300nM
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1fpf, PDBe:1fpf, PDBj:1fpf
PDBsum1fpf
PubMed7703244
UniProtP00636|F16P1_PIG Fructose-1,6-bisphosphatase 1 (Gene Name=FBP1)

[Back to BioLiP]