Structure of PDB 2q15 Chain A

Receptor sequence
>2q15A (length=385) Species: 9606 (Homo sapiens) [Search protein sequence]
EMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSSNFAVGAAPHPFLHR
YYQRQLSSTYRDLRKGVYVPYTQGKWEGELGTDLVSIPHGPQVTVRANIA
AITESDKFFIQGSNWEGILGLAYAEIARPDDSLEPFFDSLVKQTHVPNLF
SLQLCGAGFPLQQSEVLASVGGSMIIGGIDHSLYTGSLWYTPIRREWYYE
VIIVRVEINGQDLKMDCKEYNYDKSIVDSGTTNLRLPKKVFEAAVKSIKA
ASSTEKFPDGFWLGEQLVCWQAGTTPWNIFPVISLYLMGEVTQQSFRITI
LPQQYLRPVEDVATSQDDCYKFAISQSSTGTVMGAVIMEGFYVVFDRARK
RIGFAVSACHVHDEFRTAAVEGPFVTLDMEDCGYN
3D structure
PDB2q15 2-Amino-3,4-dihydroquinazolines as inhibitors of BACE-1 (beta-Site APP cleaving enzyme): Use of structure based design to convert a micromolar hit into a nanomolar lead.
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D32 S35 N37 A39 Y71 D228 T231
Catalytic site (residue number reindexed from 1) D32 S35 N37 A39 Y71 D228 T231
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 3MR A L30 D32 V69 Y71 K75 I118 D228 R235 L30 D32 V69 Y71 K75 I118 D228 R235 MOAD: Ki=11nM
PDBbind-CN: -logKd/Ki=7.96,Ki=11nM
BindingDB: Ki=8nM
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:2q15, PDBe:2q15, PDBj:2q15
PDBsum2q15
PubMed17685503
UniProtP56817|BACE1_HUMAN Beta-secretase 1 (Gene Name=BACE1)

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