Structure of PDB 2bif Chain B Binding Site BS01

Receptor Information
>2bif Chain B (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 IDF6P
InChIInChI=1S/C6H13O9P/c7-2-6(10)5(9)4(8)3(15-6)1-14-16(11,12)13/h3-5,7-10H,1-2H2,(H2,11,12,13)/t3-,4-,5+,6-/m1/s1
InChIKeyBGWGXPAPYGQALX-ARQDHWQXSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=P(O)(O)OCC1OC(O)(CO)C(O)C1O
OpenEye OEToolkits 1.5.0C(C1C(C(C(O1)(CO)O)O)O)OP(=O)(O)O
OpenEye OEToolkits 1.5.0C([C@@H]1[C@H]([C@@H]([C@](O1)(CO)O)O)O)OP(=O)(O)O
CACTVS 3.341OC[C]1(O)O[CH](CO[P](O)(O)=O)[CH](O)[CH]1O
CACTVS 3.341OC[C@@]1(O)O[C@H](CO[P](O)(O)=O)[C@@H](O)[C@@H]1O
FormulaC6 H13 O9 P
Name6-O-phosphono-beta-D-fructofuranose;
FRUCTOSE-6-PHOSPHATE;
6-O-phosphono-beta-D-fructose;
6-O-phosphono-D-fructose;
6-O-phosphono-fructose
ChEMBLCHEMBL604196
DrugBank
ZINCZINC000004096690
PDB chain2bif Chain B Residue 550 [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)
I267 G268 E325 Y336 R350 K354 Y365 Q391 R395
Binding residue
(residue number reindexed from 1)
I231 G232 E289 Y300 R314 K318 Y329 Q355 R359
Annotation score5
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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