Structure of PDB 1fta Chain A

Receptor sequence
>1ftaA (length=319) Species: 9606 (Homo sapiens) [Search protein sequence]
DVVTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAVRKAGIAHLYG
IAGVKKLDVLSNDLVMNMLKSSFATCVLVSEEDKHAIIVEPEKRGKYVVC
FDPLDGSSNIDCLVSVGTIFGIYRKKSTDEPSEKDALQPGRNLVAAGYAL
YGSATMLVLAMDCGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEAYA
KDFDPAVTEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLVYGGIFLYPA
NKKSPNGKLRLLYECNPMAYVMEKAGGMATTGKEAVLDVIPTDIHQRAPI
ILGSPDDVLEFLKVYEKHS
3D structure
PDB1fta The allosteric site of human liver fructose-1,6-bisphosphatase. Analysis of six AMP site mutants based on the crystal structure.
ChainA
Resolution2.3 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) D58 E81 E82 D102 L104 D105 E264
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 AMP A V17 E20 G21 A24 G26 T27 G28 E29 L30 T31 K112 Y113 V9 E12 G13 A16 G18 T19 G20 E21 L22 T23 K96 Y97 PDBbind-CN: -logKd/Ki=6.36,IC50=0.44uM
BindingDB: IC50=3200nM
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1fta, PDBe:1fta, PDBj:1fta
PDBsum1fta
PubMed7961695
UniProtP09467|F16P1_HUMAN Fructose-1,6-bisphosphatase 1 (Gene Name=FBP1)

[Back to BioLiP]