Structure of PDB 1c81 Chain A

Receptor sequence
>1c81A (length=191) Species: 10116 (Rattus norvegicus) [Search protein sequence]
MRSIYLCRHGESELNLRGRIGGDSGLSARGKQYAYALANFIRSQGISSLK
VWTSHMKRTIQTAEALGVPYEQWKALNEIDAGVCEEMTYEEIQEHYPEEF
ALRDQDKYRYRYPKGESYEDLVQRLEPVIMELERQENVLVICHQAVMRCL
LAYFLDKSSDELPYLKCPLHTVLKLTPVAYGCRVESIYLNV
3D structure
PDB1c81 Crystal Structure of a Trapped Phosphoenzyme During a Catalytic Reaction
ChainA
Resolution2.5 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) R257 H258 N264 R307 E327 H392
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 FDQ A R257 H258 N264 I269 R307 E327 H392 Q393 R397 R8 H9 N15 I20 R58 E78 H143 Q144 R148
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0005524 ATP binding
Biological Process
GO:0006003 fructose 2,6-bisphosphate metabolic process

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:1c81, PDBe:1c81, PDBj:1c81
PDBsum1c81
PubMed
UniProtP07953|F261_RAT 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1 (Gene Name=Pfkfb1)

[Back to BioLiP]