Structure of PDB 4rce Chain A

Receptor sequence
>4rceA (length=364) Species: 9606 (Homo sapiens) [Search protein sequence]
FVEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSSNFAVGAAPHPFL
HRYYQRQLSSTYRDLRKGVYVPYTQGKWEGELGTDLVSIPHGPNVTVRAN
IAAITESDKFFINGSNWEGILGLAYAEIARPDDSLEPFFDSLVKQTHVPN
LFSLQLCGAASVGGSMIIGGIDHSLYTGSLWYTPIRREWYYEVIIVRVEI
NGQDLKMDCKEYNYDKSIVDSGTTNLRLPKKVFEAAVKSIKAASSTEKFP
DGFWLGEQLVCWQWNIFPVISLYLMGEVTNQSFRITILPQQYLRPVDCYK
FAISQSSTGTVMGAVIMEGFYVVFDRARKRIGFAVSACHVHDEFRTAAVE
GPFVTLDMEDCGYN
3D structure
PDB4rce Lead Optimization and Modulation of hERG Activity in a Series of Aminooxazoline Xanthene beta-Site Amyloid Precursor Protein Cleaving Enzyme (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) D32 S35 N37 A39 Y71 D228 T231
Catalytic site (residue number reindexed from 1) D34 S37 N39 A41 Y73 D220 T223
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 3LN A G11 Q12 G13 L30 D32 Y71 F108 I118 D228 G230 G13 Q14 G15 L32 D34 Y73 F110 I120 D220 G222 MOAD: ic50=2nM
PDBbind-CN: -logKd/Ki=8.70,IC50=2nM
BindingDB: IC50=25nM
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:4rce, PDBe:4rce, PDBj:4rce
PDBsum4rce
PubMed25389560
UniProtP56817|BACE1_HUMAN Beta-secretase 1 (Gene Name=BACE1)

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