Structure of PDB 4xry Chain B Binding Site BS01

Receptor Information
>4xry Chain B (length=455) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GKLPPGPLPGNLLHVTPYCFDQLRRRFGDVFSLQLAWTPVVVLNGLAAVR
EALVTHGEDTADRPPVPITQILGFGPRSQGVFLARYGPAWREQRRFSVST
LRNLKSLEQWVTEEAACLCAAFANHSGRPFRPNGLLDKAVSNVIASLTCG
RRFEYDDPRFLRLLDLAQEGLKEESGFLREVLNAVPVLLHIPALAGKVLR
FQKAFLTQLDELLTEHRMTWDPAQPPRDLTEAFLAEMEKAKGNPESSFND
ENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQV
RRPEMGDQAHMPYTTAVIHEVQRFGDIVPLGVTHMTSRDIEVQGFRIPKG
TTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPEAFLPFSAGRRA
CLGEPLARMELFLFFTSLLQHFSFSVPTGQPRPSHHGVFAFLVSPSPYEL
CAVPR
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain4xry Chain A Residue 606 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4xry Utilizing Structures of CYP2D6 and BACE1 Complexes To Reduce Risk of Drug-Drug Interactions with a Novel Series of Centrally Efficacious BACE1 Inhibitors.
Resolution2.5 Å
Binding residue
(original residue number in PDB)		D422 H426
Binding residue
(residue number reindexed from 1)		D380 H384
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) T309 F436 C443
Catalytic site (residue number reindexed from 1) T267 F394 C401
Enzyme Commision number 1.14.14.-
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4xry, PDBe:4xry, PDBj:4xry
PDBsum4xry
PubMed25781223
UniProtP10635|CP2D6_HUMAN Cytochrome P450 2D6 (Gene Name=CYP2D6)

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