Structure of PDB 1yxi Chain A

Receptor sequence
>1yxiA (length=329) Species: 9823 (Sus scrofa) [Search protein sequence]
DTNIVTLTRFVMEEGRKARGTGEMTQLLNSLCTAVKAISTAVRKAGILHL
YGIAGSTNVTGDQVKKLDVLSNDLVINVLKSSFATCVLVSEEDKNAIIVE
PEKRGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKNSTDEPSEKDALQPG
RNLVAAGYALYGSATMLVLAMVNGVNCFMLDPAIGEFILVDRDVKIKKKG
SIYSINEGYAKEFDPAITEYIQRKKFPPDNSAPYGARYVGSMVADVHRTL
VYGGIFMYPANKKSPKGKLRLLYECNPMAYVMEKAGGLATTGKEAVLDIV
PTDIHQRAPIILGSPEDVTELLEIYQKHA
3D structure
PDB1yxi R-state AMP complex reveals initial steps of the quaternary transition of fructose-1,6-bisphosphatase.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D68 D74 E97 E98 D118 L120 D121 E280
Catalytic site (residue number reindexed from 1) D62 D68 E91 E92 D112 L114 D115 E274
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 F6P A D121 N212 Y215 Y244 G246 S247 M248 Y264 K274 D115 N206 Y209 Y238 G240 S241 M242 Y258 K268
BS02 MG A E97 D118 L120 E91 D112 L114
BS03 MG A D118 D121 E280 D112 D115 E274
BS04 MG A D68 E97 D62 E91
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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Cellular Component
External links
PDB RCSB:1yxi, PDBe:1yxi, PDBj:1yxi
PDBsum1yxi
PubMed15767255
UniProtP00636|F16P1_PIG Fructose-1,6-bisphosphatase 1 (Gene Name=FBP1)

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