Structure of PDB 3nsh Chain C

Receptor sequence
>3nshC (length=376) Species: 9606 (Homo sapiens) [Search protein sequence]
SFVEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSSNFAVGAAPHPF
LHRYYQRQLSSTYRDLRKGVYVPYTQGKWEGELGTDLVSIPHGPNVTVRA
NIAAITESDKFFINGSNWEGILGLAYAEIARPDDSLEPFFDSLVKQTHVP
NLFSLQLCGAGFPLNASVGGSMIIGGIDHSLYTGSLWYTPIRREWYYEVI
IVRVEINGQDLKMDCKEYNYDKSIVDSGTTNLRLPKKVFEAAVKSIKAAS
STEKFPDGFWLGEQLVCWQAGTTPWNIFPVISLYLMGEVTNQSFRITILP
QQYLRPVDDCYKFAISQSSTGTVMGAVIMEGFYVVFDRARKRIGFAVSAC
HVHDEFRTAAVEGPFVTLDMEDCGYN
3D structure
PDB3nsh Design and synthesis of hydroxyethylamine (HEA) BACE-1 inhibitors: structure-activity relationship of the aryl region.
ChainC
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D38 S41 N43 A45 Y77 D234 T237
Catalytic site (residue number reindexed from 1) D35 S38 N40 A42 Y74 D226 T229
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 957 C D38 G40 V75 P76 Y77 T78 F114 D234 G236 D35 G37 V72 P73 Y74 T75 F111 D226 G228 MOAD: ic50=470nM
BindingDB: IC50=470nM
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:3nsh, PDBe:3nsh, PDBj:3nsh
PDBsum3nsh
PubMed20822903
UniProtP56817|BACE1_HUMAN Beta-secretase 1 (Gene Name=BACE1)

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