Structure of PDB 1fkn Chain A Binding Site BS01

Receptor Information
>1fkn Chain A (length=391) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
RRGSFVEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSSNFAVGAAP
HPFLHRYYQRQLSSTYRDLRKGVYVPYTQGKWEGELGTDLVSIPHGPNVT
VRANIAAITESDKFFINGSNWEGILGLAYAEIARPDDSLEPFFDSLVKQT
HVPNLFSLQLCGAGFPLNQSEVLASVGGSMIIGGIDHSLYTGSLWYTPIR
REWYYEVIIVRVEINGQDLKMDCKEYNYDKSIVDSGTTNLRLPKKVFEAA
VKSIKAASSTEKFPDGFWLGEQLVCWQAGTTPWNIFPVISLYLMGEVTNQ
SFRITILPQQYLRPVEDVATSQDDCYKFAISQSSTGTVMGAVIMEGFYVV
FDRARKRIGFAVSACHVHDEFRTAAVEGPFVTLDMEDCGYN
Ligand information
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1fkn Structure of the protease domain of memapsin 2 (beta-secretase) complexed with inhibitor.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		G11 D32 G34 P70 Y71 T72 Q73 F108 Y198 K224 D228 G230 T231 T232 R235 T329
Binding residue
(residue number reindexed from 1)		G17 D38 G40 P76 Y77 T78 Q79 F114 Y204 K230 D234 G236 T237 T238 R241 T335
Enzymatic activity
Catalytic site (original residue number in PDB) D32 S35 N37 A39 Y71 D228 T231
Catalytic site (residue number reindexed from 1) D38 S41 N43 A45 Y77 D234 T237
Enzyme Commision number 3.4.23.46: memapsin 2.
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:1fkn, PDBe:1fkn, PDBj:1fkn
PDBsum1fkn
PubMed11021803
UniProtP56817|BACE1_HUMAN Beta-secretase 1 (Gene Name=BACE1)

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