Structure of PDB 4i12 Chain A

Receptor sequence
>4i12A (length=374) Species: 9606 (Homo sapiens) [Search protein sequence]
MVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSSNFAVGAAPHPFLHRY
YQRQLSSTYRDLRKGVYVPYTQGKWEGELGTDLVSIPHGPNVTVRANIAA
ITESDKFFINGSNWEGILGLAYAEIARPDDSLEPFFDSLVKQTHVPNLFS
LQLCGGSMIIGGIDHSLYTGSLWYTPIRREWYYEVIIVRVEINGQDLKMD
CKEYNYDKSIVDSGTTNLRLPKKVFEAAVKSIKAASSTEKFPDGFWLGEQ
LVCWQAGTTPWNIFPVISLYLMGEVTNQSFRITILPQQYLRPVTSQDDCY
KFAISQSSTGTVMGAVIMEGFYVVFDRARKRIGFAVSACHVRTAAVEGPF
VTLDMEDCGYNIPQTDESRSHHHH
3D structure
PDB4i12 Design and synthesis of thiophene dihydroisoquinolines as novel BACE1 inhibitors.
ChainA
Resolution1.78 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D93 S96 N98 A100 Y132 D289 T292
Catalytic site (residue number reindexed from 1) D31 S34 N36 A38 Y70 D212 T215
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 1BC A Q73 G74 Y132 G135 K136 K168 F169 I171 W176 G291 T292 T293 N294 Q11 G12 Y70 G73 K74 K106 F107 I109 W114 G214 T215 T216 N217 MOAD: ic50=40uM
PDBbind-CN: -logKd/Ki=6.39,IC50=0.406uM
BS02 ZN A H457 H459 H372 H374
BS03 ZN A D192 H458 D130 H373
Gene Ontology
Molecular Function
GO:0004190 aspartic-type endopeptidase activity
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0016020 membrane

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4i12, PDBe:4i12, PDBj:4i12
PDBsum4i12
PubMed23570791
UniProtP56817|BACE1_HUMAN Beta-secretase 1 (Gene Name=BACE1)

[Back to BioLiP]