Structure of PDB 1xn3 Chain C Binding Site BS01
Receptor Information
>1xn3 Chain C (length=389) Species:
9606
(Homo sapiens) [
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GSFVEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSSNFAVGAAPHP
FLHRYYQRQLSSTYRDLRKGVYVPYTQGKWEGELGTDLVSIPHGPNVTVR
ANIAAITESDKFFINGSNWEGILGLAYAEIARPDDSLEPFFDSLVKQTHV
PNLFSLQLCGAGFPLNQSEVLASVGGSMIIGGIDHSLYTGSLWYTPIRRE
WYYEVIIVRVEINGQDLKMDCKEYNYDKSIVDSGTTNLRLPKKVFEAAVK
SIKAASSTEKFPDGFWLGEQLVCWQAGTTPWNIFPVISLYLMGEVTNQSF
RITILPQQYLRPVEDVATSQDDCYKFAISQSSTGTVMGAVIMEGFYVVFD
RARKRIGFAVSACHVHDEFRTAAVEGPFVTLDMEDCGYN
Ligand information
>1xn3 Chain I (length=14) [
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KTEEISEVNLVAEF
Receptor-Ligand Complex Structure
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PDB
1xn3
Structural locations and functional roles of new subsites S5, S6, and S7 in memapsin 2 (beta-secretase).
Resolution
2.0 Å
Binding residue
(original residue number in PDB)
G11 Q12 D32 G34 S35 P70 Y71 T72 Q73 I110 W197 Y198 D223 D228 G230 T231 T232 R307 V309 K321
Binding residue
(residue number reindexed from 1)
G15 Q16 D36 G38 S39 P74 Y75 T76 Q77 I114 W201 Y202 D227 D232 G234 T235 T236 R311 V313 K325
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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Cellular Component
External links
PDB
RCSB:1xn3
,
PDBe:1xn3
,
PDBj:1xn3
PDBsum
1xn3
PubMed
15628850
UniProt
P56817
|BACE1_HUMAN Beta-secretase 1 (Gene Name=BACE1)
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