Structure of PDB 1fbt Chain B Binding Site BS01
Receptor Information
>1fbt Chain B (length=190) Species:
10116
(Rattus norvegicus) [
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RSIYLCRHGESELNLRGRIGGDSGLSARGKQYAYALANFIRSQGISSLKV
WTSHMKRTIQTAEALGVPYEQWKALNEIDAGVCEEMTYEEIQEHYPEEFA
LRDQDKYRYRYPKGESYEDLVQRLEPVIMELERQENVLVICHQAVMRCLL
AYFLDKSSDELPYLKCPLHTVLKLTPVAYGCRVESIYLNV
Ligand information
Ligand ID
PO4
InChI
InChI=1S/H3O4P/c1-5(2,3)4/h(H3,1,2,3,4)/p-3
InChIKey
NBIIXXVUZAFLBC-UHFFFAOYSA-K
SMILES
Software
SMILES
CACTVS 3.341
[O-][P]([O-])([O-])=O
ACDLabs 10.04
[O-]P([O-])([O-])=O
OpenEye OEToolkits 1.5.0
[O-]P(=O)([O-])[O-]
Formula
O4 P
Name
PHOSPHATE ION
ChEMBL
DrugBank
DB14523
ZINC
PDB chain
1fbt Chain B Residue 191 [
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Receptor-Ligand Complex Structure
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PDB
1fbt
Crystal structure of the rat liver fructose-2,6-bisphosphatase based on selenomethionine multiwavelength anomalous dispersion phases.
Resolution
2.0 Å
Binding residue
(original residue number in PDB)
R7 H8 R57 E77 H142
Binding residue
(residue number reindexed from 1)
R7 H8 R57 E77 H142
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
R7 H8 N14 R57 E77 H142
Catalytic site (residue number reindexed from 1)
R7 H8 N14 R57 E77 H142
Enzyme Commision number
2.7.1.105
: 6-phosphofructo-2-kinase.
3.1.3.46
: fructose-2,6-bisphosphate 2-phosphatase.
Gene Ontology
Molecular Function
GO:0003824
catalytic activity
GO:0005524
ATP binding
Biological Process
GO:0006003
fructose 2,6-bisphosphate metabolic process
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Molecular Function
View graph for
Biological Process
External links
PDB
RCSB:1fbt
,
PDBe:1fbt
,
PDBj:1fbt
PDBsum
1fbt
PubMed
8634242
UniProt
P07953
|F261_RAT 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1 (Gene Name=Pfkfb1)
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