Structure of PDB 4dvf Chain B

Receptor sequence
>4dvfB (length=373) Species: 9606 (Homo sapiens) [Search protein sequence]
FVEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSSNFAVGAAPHPFL
HRYYQRQLSSTYRDLRKGVYVPYTQGAWAGELGTDLVSIPHGPNVTVRAN
IAAITESDKFFINGSNWEGILGLAYAEIARPDDSLEPFFDSLVKQTHVPN
LFSLQLCGASVGGSMIIGGIDHSLYTGSLWYTPIRREWYYEVIIVRVEIN
GQDLKMDCKEYNYDKSIVDSGTTNLRLPKKVFEAAVKSIKAASSTEKFPD
GFWLGEQLVCWQAGTTPWNIFPVISLYLMGEVTNQSFRITILPQQYLRPV
ESQDDCYKFAISQSSTGTVMGAVIMEGFYVVFDRARKRIGFAVSACHVHD
EFRTAAVEGPFVTLDMEDCGYNI
3D structure
PDB4dvf Cyanobacterial Peptides as a Prototype for the Design of Potent beta-Secretase Inhibitors and the Development of Selective Chemical Probes for Other Aspartic Proteases
ChainB
Resolution1.803 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 D219 T222
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 G13 L30 D32 G34 P70 Y71 T72 Q73 F108 W115 I118 I126 W197 Y198 D228 G230 T231 T232 N233 R235 G13 Q14 G15 L32 D34 G36 P72 Y73 T74 Q75 F110 W117 I120 I128 W188 Y189 D219 G221 T222 T223 N224 R226
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:4dvf, PDBe:4dvf, PDBj:4dvf
PDBsum4dvf
PubMed23181502
UniProtP56817|BACE1_HUMAN Beta-secretase 1 (Gene Name=BACE1)

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