Structure of PDB 2zhr Chain A

Receptor sequence
>2zhrA (length=390) Species: 9606 (Homo sapiens) [Search protein sequence]
RGSFVEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSSNFAVGAAPH
PFLHRYYQRQLSSTYRDLRKGVYVPYTQGKWEGELGTDLVSIPHGPNVTV
RANIAAITESDKFFINGSNWEGILGLAYAEIARPDDSLEPFFDSLVKQTH
VPNLFSLQLCGAGFPLNQSEVLASVGGSMIIGGIDHSLYTGSLWYTPIRR
EWYYEVIIVRVEINGQDLKMDCKEYNYDKSIVDSGTTNLRLPKKVFEAAV
KSIKAASSTEKFPDGFWLGEQLVCWQAGTTPWNIFPVISLYLMGEVTNQS
FRITILPQQYLRPVEDVATSQDDCYKFAISQSSTGTVMGAVIMEGFYVVF
DRARKRIGFAVSACHVHDEFRTAAVEGPFVTLDMEDCGYN
3D structure
PDB2zhr Crystal structure of an active form of BACE1, an enzyme responsible for amyloid beta protein production
ChainA
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) D37 S40 N42 A44 Y76 D233 T236
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 A G11 Q12 D32 G34 P70 Y71 T72 Q73 I126 W197 Y198 D228 G230 T231 T232 R235 G16 Q17 D37 G39 P75 Y76 T77 Q78 I131 W202 Y203 D233 G235 T236 T237 R240
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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