Structure of PDB 4i0h Chain C

Receptor sequence
>4i0hC (length=374) Species: 9606 (Homo sapiens) [Search protein sequence]
SFVEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSSNFAVGAAPHPF
LHRYYQRQLSSTYRDLRKGVYVPYTQGKWEGELGTDLVSIPHGPNVTVRA
NIAAITESDKFFINGSNWEGILGLAYAEIARPDDSLEPFFDSLVKQTHVP
NLFSLQLCGAGFPLASVGGSMIIGGIDHSLYTGSLWYTPIRREWYYEVII
VRVEINGQDLKMDCKEYNYDKSIVDSGTTNLRLPKKVFEAAVKSIKAASS
TEKFPDGFWLGEQLVCWQAGTTPWNIFPVISLYLMGEVTNQSFRITILPQ
QYLRPVDCYKFAISQSSTGTVMGAVIMEGFYVVFDRARKRIGFAVSACHV
HDEFRTAAVEGPFVTLDMEDCGYN
3D structure
PDB4i0h SPR and structural analysis yield insight towards mechanism of inhibition of BACE inhibitors
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 D225 T228
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 1BL C D38 G40 S41 P76 Y77 T78 F114 Y204 I232 D234 G236 T238 T335 D35 G37 S38 P73 Y74 T75 F111 Y195 I223 D225 G227 T229 T318
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:4i0h, PDBe:4i0h, PDBj:4i0h
PDBsum4i0h
PubMed
UniProtP56817|BACE1_HUMAN Beta-secretase 1 (Gene Name=BACE1)

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