Structure of PDB 4gwu Chain A

Receptor sequence
>4gwuA (length=307) Species: 9823 (Sus scrofa) [Search protein sequence]
IVTLTRFVMEEGRKARGTGEMTQLLNSLCTAVKAIHRAVRKAKKLDVLSN
DLVINVLKSSFATCVLVSEEDKNAIIVEPEKRGKYVVCFDPLDGSSNIDC
LVSIGTIFGIYRKNSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLAMV
NGVNCFMYDPAIGEFILVDRDVKIKKKGSIYSINEGYAKEFDPAITEYIQ
RKKFPPDNSAPYGARYVGSMVADVHRTLVYGGIFMYPANKKSPKGKLRLL
YECNPMAYVMEKAGGLATTGKEAVLDIVPTDIHQRAPIILGSPEDVTELL
EIYQKHA
3D structure
PDB4gwu Hydrophobic Central Cavity in Fructose-1,6-bisphosphatase is Essential for the Synergism in AMP/Fru 2,6-bisphosphate Inhibition
ChainA
Resolution3.0 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) D46 E69 E70 D90 L92 D93 E252
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 FDP A D121 G122 S123 S124 N212 Y215 Y244 G246 S247 M248 Y264 K274 E280 D93 G94 S95 S96 N184 Y187 Y216 G218 S219 M220 Y236 K246 E252
BS02 MG A E97 D118 D121 E280 E69 D90 D93 E252
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:4gwu, PDBe:4gwu, PDBj:4gwu
PDBsum4gwu
PubMed
UniProtP00636|F16P1_PIG Fructose-1,6-bisphosphatase 1 (Gene Name=FBP1)

[Back to BioLiP]