Structure of PDB 6bfw Chain B

Receptor sequence
>6bfwB (length=387) Species: 9606 (Homo sapiens) [Search protein sequence]
FVEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSSNFAVGAAPHPFL
HRYYQRQLSSTYRDLRKGVYVPYTQGKWEGELGTDLVSIPHGPNVTVRAN
IAAITESDKFFINGSNWEGILGLAYAEIARPDDSLEPFFDSLVKQTHVPN
LFSLQLCGAGFPLNQSEVLASVGGSMIIGGIDHSLYTGSLWYTPIRREWY
YEVIIVRVEINGQDLKMDCKEYNYDKSIVDSGTTNLRLPKKVFEAAVKSI
KAASSTEKFPDGFWLGEQLVCWQAGTTPWNIFPVISLYLMGEVTNQSFRI
TILPQQYLRPVEDVATSQDDCYKFAISQSSTGTVMGAVIMEGFYVVFDRA
RKRIGFAVSACHVHDEFRTAAVEGPFVTLDMEDCGYN
3D structure
PDB6bfw Optimization of Hydroxyethylamine Transition State Isosteres as Aspartic Protease Inhibitors by Exploiting Conformational Preferences.
ChainB
Resolution1.84 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) D34 S37 N39 A41 Y73 D230 T233
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 DK7 B D32 G34 S35 V69 Y71 T72 F108 Y198 D228 G230 D34 G36 S37 V71 Y73 T74 F110 Y200 D230 G232 MOAD: ic50=0.22uM
Gene Ontology
Molecular Function
GO:0004190 aspartic-type endopeptidase activity
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0016020 membrane

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Biological Process
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Cellular Component
External links
PDB RCSB:6bfw, PDBe:6bfw, PDBj:6bfw
PDBsum6bfw
PubMed29088532
UniProtP56817|BACE1_HUMAN Beta-secretase 1 (Gene Name=BACE1)

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