Structure of PDB 1m4h Chain B

Receptor sequence
>1m4hB (length=389) Species: 9606 (Homo sapiens) [Search protein sequence]
GSFVEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSSNFAVGAAPHP
FLHRYYQRQLSSTYRDLRKGVYVPYTQGKWEGELGTDLVSIPHGPNVTVR
ANIAAITESDKFFINGSNWEGILGLAYAEIARPDDSLEPFFDSLVKQTHV
PNLFSLQLCGAGFPLNQSEVLASVGGSMIIGGIDHSLYTGSLWYTPIRRE
WYYEVIIVRVEINGQDLKMDCKEYNYDKSIVDSGTTNLRLPKKVFEAAVK
SIKAASSTEKFPDGFWLGEQLVCWQAGTTPWNIFPVISLYLMGEVTNQSF
RITILPQQYLRPVEDVATSQDDCYKFAISQSSTGTVMGAVIMEGFYVVFD
RARKRIGFAVSACHVHDEFRTAAVEGPFVTLDMEDCGYN
3D structure
PDB1m4h Crystal Structure of Memapsin 2 (beta-Secretase) in Complex with Inhibitor OM00-3
ChainB
Resolution2.1 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) D36 S39 N41 A43 Y75 D232 T235
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 P70 Y71 T72 Q73 F108 I110 I126 R128 Y198 D228 G230 T231 T232 R307 G15 Q16 D36 G38 P74 Y75 T76 Q77 F112 I114 I130 R132 Y202 D232 G234 T235 T236 R311
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:1m4h, PDBe:1m4h, PDBj:1m4h
PDBsum1m4h
PubMed12206667
UniProtP56817|BACE1_HUMAN Beta-secretase 1 (Gene Name=BACE1)

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