Structure of PDB 2q11 Chain C

Receptor sequence
>2q11C (length=388) Species: 9606 (Homo sapiens) [Search protein sequence]
SFVEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSSNFAVGAAPHPF
LHRYYQRQLSSTYRDLRKGVYVPYTQGKWEGELGTDLVSIPHGPQVTVRA
NIAAITESDKFFIQGSNWEGILGLAYAEIARPDDSLEPFFDSLVKQTHVP
NLFSLQLCGAGFPLQQSEVLASVGGSMIIGGIDHSLYTGSLWYTPIRREW
YYEVIIVRVEINGQDLKMDCKEYNYDKSIVDSGTTNLRLPKKVFEAAVKS
IKAASSTEKFPDGFWLGEQLVCWQAGTTPWNIFPVISLYLMGEVTQQSFR
ITILPQQYLRPVEDVATSQDDCYKFAISQSSTGTVMGAVIMEGFYVVFDR
ARKRIGFAVSACHVHDEFRTAAVEGPFVTLDMEDCGYN
3D structure
PDB2q11 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.
ChainC
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) D35 S38 N40 A42 Y74 D231 T234
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 XX4 C D32 V69 Y71 G74 K75 W76 K107 F108 D228 G230 D35 V72 Y74 G77 K78 W79 K110 F111 D231 G233 MOAD: Ki=900nM
BindingDB: Ki=900nM
Gene Ontology
Molecular Function
GO:0004190 aspartic-type endopeptidase activity
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0016020 membrane

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Cellular Component
External links
PDB RCSB:2q11, PDBe:2q11, PDBj:2q11
PDBsum2q11
PubMed17685503
UniProtP56817|BACE1_HUMAN Beta-secretase 1 (Gene Name=BACE1)

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