Structure of PDB 2fdu Chain B Binding Site BS02

Receptor Information
>2fdu Chain B (length=463) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KLPPGPTPLPFIGNYLQLNTEQMYNSLMKISERYGPVFTIHLGPRRVVVL
CGHDAVREALVDQAEEFSGRGEQATFDWVFKGYGVVFSNGERAKQLRRFS
IATLRDFGVGKRGIEERIQEEAGFLIDALRGTGGANIDPTFFLSRTVSNV
ISSIVFGDRFDYKDKEFLSLLRMMLGIFQFTSTSTGQLYEMFSSVMKHLP
GPQQQAFQLLQGLEDFIAKKVEHNQRTLDPNSPRDFIDSFLIRMQEEEKN
PNTEFYLKNLVMTTLNLFIGGTETVSTTLRYGFLLLMKHPEVEAKVHEEI
DRVIGKNRQPKFEDRAKMPYMEAVIHEIQRFGDVIPMSLARRVKKDTKFR
DFFLPKGTEVYPMLGSVLRDPSFFSNPQDFNPQHFLNEKGQFKKSDAFVP
FSIGKRNCFGEGLARMELFLFFTTVMQNFRLKSSQSPKDIDVSPKHVGFA
TIPRNYTMSFLPR
Ligand information
Ligand IDD1G
InChIInChI=1S/C12H14N2O/c1-14(2)9-11-5-6-12(15-11)10-4-3-7-13-8-10/h3-8H,9H2,1-2H3
InChIKeyPJHSLLRNPASXIS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341CN(C)Cc1oc(cc1)c2cccnc2
ACDLabs 10.04n2cccc(c1oc(cc1)CN(C)C)c2
OpenEye OEToolkits 1.5.0CN(C)Cc1ccc(o1)c2cccnc2
FormulaC12 H14 N2 O
NameN,N-DIMETHYL(5-(PYRIDIN-3-YL)FURAN-2-YL)METHANAMINE
ChEMBLCHEMBL360998
DrugBankDB07609
ZINCZINC000013607151
PDB chain2fdu Chain B Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2fdu Synthetic Inhibitors of Cytochrome P-450 2A6: Inhibitory Activity, Difference Spectra, Mechanism of Inhibition, and Protein Cocrystallization.
Resolution1.85 Å
Binding residue
(original residue number in PDB)		F107 F111 F118 N297 I300 G301 T305 F480
Binding residue
(residue number reindexed from 1)		F76 F80 F87 N266 I269 G270 T274 F449
Annotation score1
Binding affinityMOAD: Ki=14200nM
BindingDB: Ki=14200nM,IC50=2.83e+4nM
Enzymatic activity
Catalytic site (original residue number in PDB) T305 F432 C439
Catalytic site (residue number reindexed from 1) T274 F401 C408
Enzyme Commision number 1.14.14.-
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0005515 protein binding
GO:0008389 coumarin 7-hydroxylase activity
GO:0008392 arachidonate epoxygenase activity
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0016712 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
GO:0019899 enzyme binding
GO:0020037 heme binding
GO:0046872 metal ion binding
Biological Process
GO:0006629 lipid metabolic process
GO:0006805 xenobiotic metabolic process
GO:0008202 steroid metabolic process
GO:0009804 coumarin metabolic process
GO:0019373 epoxygenase P450 pathway
GO:0042178 xenobiotic catabolic process
GO:0046226 coumarin catabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005783 endoplasmic reticulum
GO:0005789 endoplasmic reticulum membrane
GO:0005881 cytoplasmic microtubule
GO:0016020 membrane
GO:0043231 intracellular membrane-bounded organelle

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2fdu, PDBe:2fdu, PDBj:2fdu
PDBsum2fdu
PubMed17125252
UniProtP11509|CP2A6_HUMAN Cytochrome P450 2A6 (Gene Name=CYP2A6)

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