Structure of PDB 4xrz Chain A

Receptor sequence
>4xrzA (length=457) Species: 9606 (Homo sapiens) [Search protein sequence]
GKLPPGPLPDFQNTPYCFDQLRRRFGDVFSLQLAWTPVVVLNGLAAVREA
LVTHGEDTADRPPVPITQILGFGPRSQGVFLARYGPAWREQRRFSVSTLR
NLGLGKKSLEQWVTEEAACLCAAFANHSGRPFRPNGLLDKAVSNVIASLT
CGRRFEYDDPRFLRLLDLAQEGLKEESGFLREVLNAVPVLLHIPALAGKV
LRFQKAFLTQLDELLTEHRMTWDPAQPPRDLTEAFLAEMEKAKGNPESSF
NDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIG
QVRRPEMGDQAHMPYTTAVIHEVQRFGDIVPLGVTHMTSRDIEVQGFRIP
KGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPEAFLPFSAGR
RACLGEPLARMELFLFFTSLLQHFSFSVPTGQPRPSHHGVFAFLVSPSPY
ELCAVPR
3D structure
PDB4xrz Utilizing Structures of CYP2D6 and BACE1 Complexes To Reduce Risk of Drug-Drug Interactions with a Novel Series of Centrally Efficacious BACE1 Inhibitors.
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T309 F436 C443
Catalytic site (residue number reindexed from 1) T269 F396 C403
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 V119 F120 W128 R132 A305 T309 V374 H376 P435 F436 S437 R441 C443 L444 G445 R61 V79 F80 W88 R92 A265 T269 V334 H336 P395 F396 S397 R401 C403 L404 G405
BS02 SI6 A F120 G212 L213 E216 D301 S304 A305 T309 F483 F80 G172 L173 E176 D261 S264 A265 T269 F443 MOAD: ic50=0.37uM
BindingDB: IC50=370nM
BS03 ZN A H258 D270 E273 H218 D230 E233
BS04 ZN A D422 H426 D382 H386
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0016491 oxidoreductase 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:0020037 heme binding
GO:0046872 metal ion binding
GO:0062187 anandamide 8,9 epoxidase activity
GO:0062188 anandamide 11,12 epoxidase activity
GO:0062189 anandamide 14,15 epoxidase activity
Biological Process
GO:0006631 fatty acid metabolic process
GO:0006805 xenobiotic metabolic process
GO:0008202 steroid metabolic process
GO:0008203 cholesterol metabolic process
GO:0008210 estrogen metabolic process
GO:0009804 coumarin metabolic process
GO:0009820 alkaloid metabolic process
GO:0009822 alkaloid catabolic process
GO:0016098 monoterpenoid metabolic process
GO:0019369 arachidonate metabolic process
GO:0033076 isoquinoline alkaloid metabolic process
GO:0042178 xenobiotic catabolic process
GO:0042572 retinol metabolic process
GO:0042759 long-chain fatty acid biosynthetic process
GO:0051100 negative regulation of binding
GO:0070989 oxidative demethylation
GO:0090350 negative regulation of cellular organofluorine metabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005783 endoplasmic reticulum
GO:0005789 endoplasmic reticulum membrane
GO:0016020 membrane
GO:0043231 intracellular membrane-bounded organelle

View graph for
Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4xrz, PDBe:4xrz, PDBj:4xrz
PDBsum4xrz
PubMed25781223
UniProtP10635|CP2D6_HUMAN Cytochrome P450 2D6 (Gene Name=CYP2D6)

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