Structure of PDB 5tfu Chain D

Receptor sequence
>5tfuD (length=453) Species: 9606 (Homo sapiens) [Search protein sequence]
LPPGPLPQNTPYCFDQLRRRFGDVFSLQLAWTPVVVLNGLAAVREALVTH
GEDTADRPPVPITQILGFGPRSQGVFLARYGPAWREQRRFSVSTLRNLGL
GKKSLEQWVTEEAACLCAAFANHSGRPFRPNGLLDKAVSNVIASLTCGRR
FEYDDPRFLRLLDLAQEGLKEESGFLREVLNAVPVLLHIPALAGKVLRFQ
KAFLTQLDELLTEHRMTWDPAQPPRDLTEAFLAEMEKAKGNPESSFNDEN
LRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRR
PEMGDQAHMPYTTAVIHEVQRFGDIVPLGVTHMTSRDIEVQGFRIPKGTT
LITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPEAFLPFSAGRRACL
GEPLARMELFLFFTSLLQHFSFSVPTGQPRPSHHGVFAFLVSPSPYELCA
VPR
3D structure
PDB5tfu Aminomethyl-Derived Beta Secretase (BACE1) Inhibitors: Engaging Gly230 without an Anilide Functionality.
ChainD
Resolution2.75 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) T265 F392 C399
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 D R101 F120 R132 A305 G306 T309 V374 H376 P435 F436 S437 R441 C443 L444 G445 R57 F76 R88 A261 G262 T265 V330 H332 P391 F392 S393 R397 C399 L400 G401
BS02 ZN D H258 D270 E273 H214 D226 E229
BS03 P6M D F120 A209 E216 Q244 L248 D301 S304 A305 F76 A165 E172 Q200 L204 D257 S260 A261 BindingDB: IC50=334nM
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
View graph for
Cellular Component
External links
PDB RCSB:5tfu, PDBe:5tfu, PDBj:5tfu
PDBsum5tfu
PubMed27997172
UniProtP10635|CP2D6_HUMAN Cytochrome P450 2D6 (Gene Name=CYP2D6)

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