Structure of PDB 3uqu Chain A

Receptor sequence
>3uquA (length=374) Species: 9606 (Homo sapiens) [Search protein sequence]
RGSFVEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSSNFAVGAAPH
PFLHRYYQRQLSSTYRDLRKGVYVPYTQGAWAGELGTDLVSIPHGPNVTV
RANIAAITESDKFFINGSNWEGILGLAYAEIARPDDSLEPFFDSLVKQTH
VPNLFSLQLCGAVGGSMIIGGIDHSLYTGSLWYTPIRREWYYEVIIVRVE
INGQDLKMDCKEYNYDKSIVDSGTTNLRLPKKVFEAAVKSIKAASSTEKF
PDGFWLGEQLVCWQAGTTPWNIFPVISLYLMGEVTNQSFRITILPQQYLR
PVESQDDCYKFAISQSSTGTVMGAVIMEGFYVVFDRARKRIGFAVSACHV
HDEFRTAAVEGPFVTLDMEDCGYN
3D structure
PDB3uqu Flexibility of the Flap in the Active Site of BACE1 as Revealed by Crystal Structures and MD simulations
ChainA
Resolution1.7 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 D221 T224
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 ZPX A Q12 G13 L30 D32 Y71 T72 Q73 F108 W115 D228 G230 T232 N233 R235 A335 Q17 G18 L35 D37 Y76 T77 Q78 F113 W120 D221 G223 T225 N226 R228 A324
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:3uqu, PDBe:3uqu, PDBj:3uqu
PDBsum3uqu
PubMed
UniProtP56817|BACE1_HUMAN Beta-secretase 1 (Gene Name=BACE1)

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