Structure of PDB 2fdu Chain A

Receptor sequence
>2fduA (length=465) Species: 9606 (Homo sapiens) [Search protein sequence]
KGKLPPGPTPLPFIGNYLQLNTEQMYNSLMKISERYGPVFTIHLGPRRVV
VLCGHDAVREALVDQAEEFSGRGEQATFDWVFKGYGVVFSNGERAKQLRR
FSIATLRDFGVGKRGIEERIQEEAGFLIDALRGTGGANIDPTFFLSRTVS
NVISSIVFGDRFDYKDKEFLSLLRMMLGIFQFTSTSTGQLYEMFSSVMKH
LPGPQQQAFQLLQGLEDFIAKKVEHNQRTLDPNSPRDFIDSFLIRMQEEE
KNPNTEFYLKNLVMTTLNLFIGGTETVSTTLRYGFLLLMKHPEVEAKVHE
EIDRVIGKNRQPKFEDRAKMPYMEAVIHEIQRFGDVIPMSLARRVKKDTK
FRDFFLPKGTEVYPMLGSVLRDPSFFSNPQDFNPQHFLNEKGQFKKSDAF
VPFSIGKRNCFGEGLARMELFLFFTTVMQNFRLKSSQSPKDIDVSPKHVG
FATIPRNYTMSFLPR
3D structure
PDB2fdu Synthetic Inhibitors of Cytochrome P-450 2A6: Inhibitory Activity, Difference Spectra, Mechanism of Inhibition, and Protein Cocrystallization.
ChainA
Resolution1.85 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T305 F432 C439
Catalytic site (residue number reindexed from 1) T276 F403 C410
Enzyme Commision number 1.14.14.-
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 HEM A R101 V117 R128 G301 G302 T305 R372 P431 F432 S433 R437 C439 F440 G441 R72 V88 R99 G272 G273 T276 R343 P402 F403 S404 R408 C410 F411 G412
BS02 D1G A F107 F111 N297 I300 G301 T305 F480 F78 F82 N268 I271 G272 T276 F451 MOAD: Ki=14200nM
BindingDB: Ki=14200nM,IC50=2.83e+4nM
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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