Structure of PDB 1ym2 Chain C Binding Site BS01
Receptor Information
>1ym2 Chain C (length=376) Species:
9606
(Homo sapiens) [
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SFVEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSSNFAVGAAPHPF
LHRYYQRQLSSTYRDLRKGVYVPYTQGKWEGELGTDLVSIPHGPNVTVRA
NIAAITESDKFFINGSNWEGILGLAYAEIARPDDSLEPFFDSLVKQTHVP
NLFSLQLCGAVGGSMIIGGIDHSLYTGSLWYTPIRREWYYEVIIVRVEIN
GQDLKMDCKEYNYDKSIVDSGTTNLRLPKKVFEAAVKSIKAASSTEKFPD
GFWLGEQLVCWQAGTTPWNIFPVISLYLMGEVTNQSFRITILPQQYLRPV
EDVATSQDDCYKFAISQSSTGTVMGAVIMEGFYVVFDRARKRIGFAVSAC
HVHDEFRTAAVEGPFVTLDMEDCGYN
Ligand information
>1ym2 Chain Z (length=3) [
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LMV
Receptor-Ligand Complex Structure
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PDB
1ym2
Structure-based design, synthesis, and memapsin 2 (BACE) inhibitory activity of carbocyclic and heterocyclic peptidomimetics
Resolution
2.05 Å
Binding residue
(original residue number in PDB)
G13 D32 G34 P70 Y71 T72 Q73 I126 Y198 D228 G230 T231 T232 R235
Binding residue
(residue number reindexed from 1)
G16 D35 G37 P73 Y74 T75 Q76 I129 Y189 D219 G221 T222 T223 R226
Enzymatic activity
Catalytic site (original residue number in PDB)
D32 S35 N37 A39 Y71 D228 T231
Catalytic site (residue number reindexed from 1)
D35 S38 N40 A42 Y74 D219 T222
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:1ym2
,
PDBe:1ym2
,
PDBj:1ym2
PDBsum
1ym2
PubMed
16078837
UniProt
P56817
|BACE1_HUMAN Beta-secretase 1 (Gene Name=BACE1)
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