Structure of PDB 2bif Chain A Binding Site BS02

Receptor Information
>2bif Chain A (length=432) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
CPTLIVMVGLPARGKTYISKKLTRYLNFIGVPTREFNVGQYRRDMVKTYK
SFEFFLPDNEEGLKIRKQCALAALNDVRKFLSEEGGHVAVFDATNTTRER
RAMIFNFGEQNGYKTFFVESICVDPEVIAANIVQVKLGSPDYVNRDSDEA
TEDFMRRIECYENSYESLDEEQDRDLSYIKIMDVGQSYVVNRVADHIQSR
IVYYLMNIHVTPRSIYLCRAGESELNLKGRIGGDPGLSPRGREFSKHLAQ
FISDQNIKDLKVFTSQMKRTIQTAEALSVPYEQFKVLNEIDAGVCEEMTY
EEIQDHYPLEFALRDQDKYRYRYPKGESYEDLVQRLEPVIMELERQENVL
VICHQAVMRCLLAYFLDKAAEELPYLKCPLHTVLKLTPVAYGCKVESIFL
NVAAVNTHRDRPQNVDISRPSEEALVTVPAHQ
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain2bif Chain A Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2bif Crystal structure of the H256A mutant of rat testis fructose-6-phosphate,2-kinase/fructose-2,6-bisphosphatase. Fructose 6-phosphate in the active site leads to mechanisms for both mutant and wild type bisphosphatase activities.
Resolution2.4 Å
Binding residue
(original residue number in PDB)		K51 T52 D128
Binding residue
(residue number reindexed from 1)		K15 T16 D92
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) R255 A256 N262 R305 E325 H390
Catalytic site (residue number reindexed from 1) R219 A220 N226 R269 E289 H354
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:0003873 6-phosphofructo-2-kinase activity
GO:0004331 fructose-2,6-bisphosphate 2-phosphatase activity
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0016787 hydrolase activity
Biological Process
GO:0006000 fructose metabolic process
GO:0006003 fructose 2,6-bisphosphate metabolic process
GO:0016310 phosphorylation
GO:0046835 carbohydrate phosphorylation
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2bif, PDBe:2bif, PDBj:2bif
PDBsum2bif
PubMed9890980
UniProtP25114|F264_RAT 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4 (Gene Name=Pfkfb4)

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