Structure of PDB 2zhr Chain B

Receptor sequence
>2zhrB (length=385) Species: 9606 (Homo sapiens) [Search protein sequence]
FVEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSSNFAVGAAPHPFL
HRYYQRQLSSTYRDLRKGVYVPYTQGKWEGELGTDLVSIPHGPNVTVRAN
IAAITESDKFFINGSNWEGILGLAYAEIARPDDSLEPFFDSLVKQTHVPN
LFSLQLCGAGFPLNQSEVLASVGGSMIIGGIDHSLYTGSLWYTPIRREWY
YEVIIVRVEINGQDLKMDCKEYNYDKSIVDSGTTNLRLPKKVFEAAVKSI
KAASSTEKFPDGFWLGEQLVCWQAGTTPWNIFPVISLYLMGEVTNQSFRI
TILPQQYLRPVEDVSQDDCYKFAISQSSTGTVMGAVIMEGFYVVFDRARK
RIGFAVSACHVHDEFRTAAVEGPFVTLDMEDCGYN
3D structure
PDB2zhr Crystal structure of an active form of BACE1, an enzyme responsible for amyloid beta protein production
ChainB
Resolution2.5 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 peptide B G11 Q12 D32 G34 Y71 T72 Q73 E125 I126 Y198 D228 G230 T231 T232 R235 G13 Q14 D34 G36 Y73 T74 Q75 E127 I128 Y200 D230 G232 T233 T234 R237
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:2zhr, PDBe:2zhr, PDBj:2zhr
PDBsum2zhr
PubMed18378702
UniProtP56817|BACE1_HUMAN Beta-secretase 1 (Gene Name=BACE1)

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