Structure of PDB 1fta Chain C
Receptor sequence
>1ftaC (length=317) Species:
9606
(Homo sapiens) [
Search protein sequence
]
DVVTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAVRKAGIAHLYG
IAGKLDVLSNDLVMNMLKSSFATCVLVSEEDKHAIIVEPEKRGKYVVCFD
PLDGSSNIDCLVSVGTIFGIYRKKSTDEPSEKDALQPGRNLVAAGYALYG
SATMLVLAMDCGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEAYAKD
FDPAVTEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLVYGGIFLYPANK
KSPNGKLRLLYECNPMAYVMEKAGGMATTGKEAVLDVIPTDIHQRAPIIL
GSPDDVLEFLKVYEKHS
3D structure
PDB
1fta
The allosteric site of human liver fructose-1,6-bisphosphatase. Analysis of six AMP site mutants based on the crystal structure.
Chain
C
Resolution
2.3 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)
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
AMP
C
V17 E20 G21 A24 G26 T27 G28 E29 L30 K112 Y113 R140 M177
V9 E12 G13 A16 G18 T19 G20 E21 L22 K94 Y95 R122 M159
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
PDBsum
1fta
PubMed
7961695
UniProt
P09467
|F16P1_HUMAN Fructose-1,6-bisphosphatase 1 (Gene Name=FBP1)
[
Back to BioLiP
]