Structure of PDB 5htk Chain B Binding Site BS02

Receptor Information
>5htk Chain B (length=420) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ASYMTNSPTLIVMIGLPARGKTYVSKKLTRYLNWIGVPTKVFNLGVYRRE
AVKSYKSYDFFRHDNEEAMKIRKQCALVALEDVKAYLTEENGQIAVFDAT
NTTRERRDMILNFAEQNSFKVFFVESVCDDPDVIAANILEVKVSSPDYPE
RNRENVMEDFLKRIECYKVTYRPLDPDNYDKDLSFIKVINVGQRFLVNRV
QDYIQSKIVYYLMNIHVQPRTIYLCRHGESEFNLLGKIGGDSGLSVRGKQ
FAQALRKFLEEQEITDLKVWTSQLKRTIQTAESLGVPYEQWKILNEIDAG
VCEEMTYAEIEKRYPEEFALRDQEKYLYRYPGGESYQDLVQRLEPVIMEL
ERQGNVLVISHQAVMRCLLAYFLDKGADELPYLRCPLHTIFKLTPVAYGC
KVETIKLNVEAVNTHRDKPT
Ligand information
Ligand IDATP
InChIInChI=1S/C10H16N5O13P3/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(26-10)1-25-30(21,22)28-31(23,24)27-29(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H,23,24)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
InChIKeyZKHQWZAMYRWXGA-KQYNXXCUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OP(=O)(O)O)O)O)N
CACTVS 3.341Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(=O)O[P](O)(O)=O)[CH](O)[CH]3O
ACDLabs 10.04O=P(O)(O)OP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@@](=O)(O)O[P@](=O)(O)OP(=O)(O)O)O)O)N
CACTVS 3.341Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@](O)(=O)O[P@@](O)(=O)O[P](O)(O)=O)[C@@H](O)[C@H]3O
FormulaC10 H16 N5 O13 P3
NameADENOSINE-5'-TRIPHOSPHATE
ChEMBLCHEMBL14249
DrugBankDB00171
ZINCZINC000004261765
PDB chain5htk Chain B Residue 602 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB5htk Crystal structure of heart 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB2) and the inhibitory influence of citrate on substrate binding.
Resolution2.01 Å
Binding residue
(original residue number in PDB)		P47 A48 R49 G50 K51 T52 E170 S174 S175 P176 F190 A427 Y428
Binding residue
(residue number reindexed from 1)		P17 A18 R19 G20 K21 T22 E140 S144 S145 P146 F160 A397 Y398
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) R256 H257 N263 R306 E326 H391
Catalytic site (residue number reindexed from 1) R226 H227 N233 R276 E296 H361
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:0005515 protein binding
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0016787 hydrolase activity
GO:0019900 kinase binding
GO:0019901 protein kinase binding
Biological Process
GO:0006000 fructose metabolic process
GO:0006003 fructose 2,6-bisphosphate metabolic process
GO:0006007 glucose catabolic process
GO:0006089 lactate metabolic process
GO:0006090 pyruvate metabolic process
GO:0006096 glycolytic process
GO:0009749 response to glucose
GO:0016310 phosphorylation
GO:0032024 positive regulation of insulin secretion
GO:0046835 carbohydrate phosphorylation
Cellular Component
GO:0005654 nucleoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5htk, PDBe:5htk, PDBj:5htk
PDBsum5htk
PubMed27802586
UniProtO60825|F262_HUMAN 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2 (Gene Name=PFKFB2)

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