Structure of PDB 3kyr Chain B

Receptor sequence
>3kyrB (length=363) Species: 9606 (Homo sapiens) [Search protein sequence]
SFVEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSSNFAVGAAPHPF
LHRYYQRQLSSTYRDLRKGVYVPYTQGKWEGELGTDLVSIPHGPNVTVRA
NIAAITESDKFFINGSNWEGILGLAYAEIARPDDSLEPFFDSLVKQTHVP
NLFSLQLCGASVGGSMIIGGIDHSLYTGSLWYTPIRREWYYEVIIVRVEI
NGQDLKMDCKEYNYDKSIVDSGTTNLRLPKKVFEAAVKSIKAASSTEDGF
WLGEQLVCWQAGTTPWNIFPVISLYLMGEVTNQSFRITILPQQYLRPDDC
YKFAISQSSTGTVMGAVIMEGFYVVFDRARKRIGFAVSACHVHDEFRTAA
VEGPFVTLDMEDC
3D structure
PDB3kyr Investigation of a-phenylnorstatine and a-benzylnorstatine as transition state isostere motifs in the search for new BACE-1 inhibiotrs
ChainB
Resolution2.6 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) D35 S38 N40 A42 Y74 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 038 B G34 Y68 P70 Y71 T72 R128 Y198 D228 R235 T329 G37 Y71 P73 Y74 T75 R131 Y190 D220 R227 T310 BindingDB: IC50=190nM
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:3kyr, PDBe:3kyr, PDBj:3kyr
PDBsum3kyr
PubMed
UniProtP56817|BACE1_HUMAN Beta-secretase 1 (Gene Name=BACE1)

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