Structure of PDB 3ru1 Chain A

Receptor sequence
>3ru1A (length=363) Species: 9606 (Homo sapiens) [Search protein sequence]
FVEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSSNFAVGAAPHPFL
HRYYQRQLSSTYRDLRKGVYVPYTQGKWEGELGTDLVSIPHGPNVTVRAN
IAAITESDKFFINGSNWEGILGLAYAEIARPDDSLEPFFDSLVKQTHVPN
LFSLQLCGASVGGSMIIGGIDHSLYTGSLWYTPIRREWYYEVIIVRVEIN
GQDLKMDCKEYNYDKSIVDSGTTNLRLPKKVFEAAVKSIKAASSTEKFPD
GFWLGEQLVCWQNIFPVISLYLMGEVTNQSFRITILPQQYLRPVEDCYKF
AISQSSTGTVMGAVIMEGFYVVFDRARKRIGFAVSACHVHDEFRTAAVEG
PFVTLDMEDCGYN
3D structure
PDB3ru1 From Fragment Screening to In Vivo Efficacy: Optimization of a Series of 2-Aminoquinolines as Potent Inhibitors of Beta-Site Amyloid Precursor Protein Cleaving Enzyme 1 (BACE1).
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D32 S35 N37 A39 Y71 D228 T231
Catalytic site (residue number reindexed from 1) D34 S37 N39 A41 Y73 D219 T222
Enzyme Commision number 3.4.23.46: memapsin 2.
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 3RU A D32 G34 S35 V69 Y71 Y198 D228 D34 G36 S37 V71 Y73 Y189 D219 MOAD: Kd=14.2uM
PDBbind-CN: -logKd/Ki=4.85,Kd=14.2uM
BindingDB: Kd=14200nM
Gene Ontology
Molecular Function
GO:0004190 aspartic-type endopeptidase activity
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3ru1, PDBe:3ru1, PDBj:3ru1
PDBsum3ru1
PubMed21707077
UniProtP56817|BACE1_HUMAN Beta-secretase 1 (Gene Name=BACE1)

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