Structure of PDB 1fbt Chain A

Receptor sequence
>1fbtA (length=190) Species: 10116 (Rattus norvegicus) [Search protein sequence]
RSIYLCRHGESELNLRGRIGGDSGLSARGKQYAYALANFIRSQGISSLKV
WTSHMKRTIQTAEALGVPYEQWKALNEIDAGVCEEMTYEEIQEHYPEEFA
LRDQDKYRYRYPKGESYEDLVQRLEPVIMELERQENVLVICHQAVMRCLL
AYFLDKSSDELPYLKCPLHTVLKLTPVAYGCRVESIYLNV
3D structure
PDB1fbt Crystal structure of the rat liver fructose-2,6-bisphosphatase based on selenomethionine multiwavelength anomalous dispersion phases.
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) 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.
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 PO4 A R7 H8 R57 E77 H142 Q143 R7 H8 R57 E77 H142 Q143
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
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Biological Process
External links
PDB RCSB:1fbt, PDBe:1fbt, PDBj:1fbt
PDBsum1fbt
PubMed8634242
UniProtP07953|F261_RAT 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1 (Gene Name=Pfkfb1)

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