Structure of PDB 2bif Chain A

Receptor sequence
>2bifA (length=432) Species: 10116 (Rattus norvegicus) [Search protein sequence]
CPTLIVMVGLPARGKTYISKKLTRYLNFIGVPTREFNVGQYRRDMVKTYK
SFEFFLPDNEEGLKIRKQCALAALNDVRKFLSEEGGHVAVFDATNTTRER
RAMIFNFGEQNGYKTFFVESICVDPEVIAANIVQVKLGSPDYVNRDSDEA
TEDFMRRIECYENSYESLDEEQDRDLSYIKIMDVGQSYVVNRVADHIQSR
IVYYLMNIHVTPRSIYLCRAGESELNLKGRIGGDPGLSPRGREFSKHLAQ
FISDQNIKDLKVFTSQMKRTIQTAEALSVPYEQFKVLNEIDAGVCEEMTY
EEIQDHYPLEFALRDQDKYRYRYPKGESYEDLVQRLEPVIMELERQENVL
VICHQAVMRCLLAYFLDKAAEELPYLKCPLHTVLKLTPVAYGCKVESIFL
NVAAVNTHRDRPQNVDISRPSEEALVTVPAHQ
3D structure
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.
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 F6P A I267 G268 E325 Y336 R350 K354 Y365 Q391 R395 T443 I231 G232 E289 Y300 R314 K318 Y329 Q355 R359 T407
BS02 MG A K51 T52 D128 K15 T16 D92
BS03 PO4 A R255 N262 R305 H390 R219 N226 R269 H354
BS04 ANP A P47 A48 R49 G50 K51 T52 Y53 N167 V220 Y427 P11 A12 R13 G14 K15 T16 Y17 N131 V184 Y391
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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