Structure of PDB 1fpi Chain A Binding Site BS01
Receptor Information
>1fpi Chain A (length=317) Species:
9823
(Sus scrofa) [
Search protein sequence
] [
Download receptor structure
] [
Download structure with residue number starting from 1
] [
View receptor structure
]
NIVTLTRFVMEQGRKARGTGEMTQLLNSLCTAVKAISTAVRKAGIAHLYG
IAGKLDVLSNDLVINVLKSSFATCVLVTEEDKNAIIVEPEKRGKYVVCFD
PLDGSSNIDCLVSIGTIFGIYRKNSTDEPSEKDALQPGRNLVAAGYALYG
SATMLVLAMVNGVNCFMLDPAIGEFILVDRNVKIKKKGSIYSINEGYAKE
FDPAITEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLVYGGIFMYPANK
KSPKGKLRLLYECNPMAYVMEKAGGLATTGKEAVLDIVPTDIHQRAPIIL
GSPEDVTELLEIYQKHA
Ligand information
Ligand ID
K
InChI
InChI=1S/K/q+1
InChIKey
NPYPAHLBTDXSSS-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0
[K+]
Formula
K
Name
POTASSIUM ION
ChEMBL
CHEMBL1233793
DrugBank
DB01345
ZINC
PDB chain
1fpi Chain A Residue 336 [
Download ligand structure
] [
Download structure with residue number starting from 1
] [
View ligand structure
]
Receptor-Ligand Complex Structure
Global view
Local view
Structure summary
[
Spin on
] [
Spin off
] [
Reset
]
[
High quality
] [
Low quality
]
[
White background
] [
Black background
]
[
Spin on
] [
Spin off
] [
Reset
]
[
High quality
] [
Low quality
]
[
White background
] [
Black background
]
PDB
1fpi
Crystallographic evidence for the action of potassium, thallium, and lithium ions on fructose-1,6-bisphosphatase.
Resolution
2.3 Å
Binding residue
(original residue number in PDB)
E97 E98 D118 L120 D121 S123
Binding residue
(residue number reindexed from 1)
E79 E80 D100 L102 D103 S105
Annotation score
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.
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:1fpi
,
PDBe:1fpi
,
PDBj:1fpi
PDBsum
1fpi
PubMed
7568043
UniProt
P00636
|F16P1_PIG Fructose-1,6-bisphosphatase 1 (Gene Name=FBP1)
[
Back to BioLiP
]