Structure of PDB 1c80 Chain A

Receptor sequence
>1c80A (length=191) Species: 10116 (Rattus norvegicus) [Search protein sequence]
MRSIYLCRHGESELNLRGRIGGDSGLSARGKQYAYALANFIRSQGISSLK
VWTSHMKRTIQTAEALGVPYEQWKALNEIDAGVCEEMTYEEIQEHYPEEF
ALRDQDKYRYRYPKGESYEDLVQRLEPVIMELERQENVLVICHQAVMRCL
LAYFLDKSSDELPYLKCPLHTVLKLTPVAYGCRVESIYLNV
3D structure
PDB1c80 Crystal Structure of a Trapped Phosphoenzyme During a Catalytic Reaction
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R8 H9 N15 R58 E78 H143
Catalytic site (residue number reindexed from 1) R8 H9 N15 R58 E78 H143
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 GTP A I20 E78 I79 Y89 F100 R103 Y112 Y118 Q144 A145 R148 I20 E78 I79 Y89 F100 R103 Y112 Y118 Q144 A145 R148
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:1c80, PDBe:1c80, PDBj:1c80
PDBsum1c80
PubMed
UniProtP07953|F261_RAT 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1 (Gene Name=Pfkfb1)

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