Structure of PDB 1fkn Chain B Binding Site BS01
Receptor Information
>1fkn Chain B (length=389) Species:
9606
(Homo sapiens) [
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GSFVEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSSNFAVGAAPHP
FLHRYYQRQLSSTYRDLRKGVYVPYTQGKWEGELGTDLVSIPHGPNVTVR
ANIAAITESDKFFINGSNWEGILGLAYAEIARPDDSLEPFFDSLVKQTHV
PNLFSLQLCGAGFPLNQSEVLASVGGSMIIGGIDHSLYTGSLWYTPIRRE
WYYEVIIVRVEINGQDLKMDCKEYNYDKSIVDSGTTNLRLPKKVFEAAVK
SIKAASSTEKFPDGFWLGEQLVCWQAGTTPWNIFPVISLYLMGEVTNQSF
RITILPQQYLRPVEDVATSQDDCYKFAISQSSTGTVMGAVIMEGFYVVFD
RARKRIGFAVSACHVHDEFRTAAVEGPFVTLDMEDCGYN
Ligand information
>1fkn Chain D (length=7) [
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EVNGAEF
Receptor-Ligand Complex Structure
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PDB
1fkn
Structure of the protease domain of memapsin 2 (beta-secretase) complexed with inhibitor.
Resolution
1.9 Å
Binding residue
(original residue number in PDB)
G11 D32 G34 Y71 T72 Q73 F108 Y198 D228 G230 T231 T232 R235 T329
Binding residue
(residue number reindexed from 1)
G15 D36 G38 Y75 T76 Q77 F112 Y202 D232 G234 T235 T236 R239 T333
Enzymatic activity
Catalytic site (original residue number in PDB)
D32 S35 N37 A39 Y71 D228 T231
Catalytic site (residue number reindexed from 1)
D36 S39 N41 A43 Y75 D232 T235
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
PDBsum
1fkn
PubMed
11021803
UniProt
P56817
|BACE1_HUMAN Beta-secretase 1 (Gene Name=BACE1)
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