Structure of PDB 4ma4 Chain A Binding Site BS01

Receptor Information
>4ma4 Chain A (length=444) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LELTQSRVQKIWVPVDHRPSLPNSPTVIVMVGLPARGKTYISKKLTRYLN
WIGVPTKVFNVGEYRREAVKQYSSYNFFRPDNEEAMKVRKQCALAALRDV
KSYLAKEGGQIAVFDATNTTRERRHMILHFAKENDFKAFFIESVCDDPTV
VASNIMEVKISSPDYKDCNSAEAMDDFMKRISCYEASYQPLDPDKCDRDL
SLIKVIDVGRRFLVNRVQDHIQSRIVYYLMNIHVQPRTIYLCRHGENEHN
LQGRIGGDSGLSSRGKKFASALSKFVEEQNLKDLRVWTSQLKSTIQTAEA
LRLPYEQWKALNEIDAGVCEELTYEEIRDTYPEEYALREQDKYYYRYPTG
ESYQDLVQRLEPVIMELERQENVLVICHQAVLRCLLAYFLDKSAEEMPYL
KCPLHTVLKLTPVAYGCRVESIYLNVESVCTHRERSNPLMRRNS
Ligand information
Ligand IDADP
InChIInChI=1S/C10H15N5O10P2/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(24-10)1-23-27(21,22)25-26(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
InChIKeyXTWYTFMLZFPYCI-KQYNXXCUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=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)[CH](O)[CH]3O
ACDLabs 10.04O=P(O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
CACTVS 3.341Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@@](O)(=O)O[P](O)(O)=O)[C@@H](O)[C@H]3O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)O)O)O)N
FormulaC10 H15 N5 O10 P2
NameADENOSINE-5'-DIPHOSPHATE
ChEMBLCHEMBL14830
DrugBankDB16833
ZINCZINC000012360703
PDB chain4ma4 Chain A Residue 601 [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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PDB4ma4 PFKFB3 Regulates Oxidative Stress Homeostasis via Its S-Glutathionylation in Cancer.
Resolution2.23 Å
Binding residue
(original residue number in PDB)		A44 R45 G46 K47 T48 Y49 S152 N163 V167 K168 Y424
Binding residue
(residue number reindexed from 1)		A35 R36 G37 K38 T39 Y40 S143 N154 V158 K159 Y415
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) R252 H253 N259 S302 E322 H387
Catalytic site (residue number reindexed from 1) R243 H244 N250 S293 E313 H378
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
Biological Process
GO:0006000 fructose metabolic process
GO:0006003 fructose 2,6-bisphosphate metabolic process
GO:0006096 glycolytic process
GO:0006915 apoptotic process
GO:0010001 glial cell differentiation
GO:0016310 phosphorylation
GO:0046835 carbohydrate phosphorylation
GO:0061744 motor behavior
Cellular Component
GO:0005654 nucleoplasm
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:4ma4, PDBe:4ma4, PDBj:4ma4
PDBsum4ma4
PubMed24295899
UniProtQ16875|F263_HUMAN 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 (Gene Name=PFKFB3)

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