Structure of PDB 7d5b Chain A

Receptor sequence
>7d5bA (length=369) Species: 9606 (Homo sapiens) [Search protein sequence]
ANFLAMVDNLQGDSGRGYYLEMLIGTPPQKLQILVDTGSSNFAVAGTPHS
YIDTYFDTERSSTYRSKGFDVTVKYTQGSWTGFVGEDLVTIPKGFNTSFL
VNIATIFESENFFLPGIKWNGILGLAYATLAKPSSSLETFFDSLVTQANI
PNVFSMQMCGAGLNGGSLVLGGIEPSLYKGDIWYTPIKEEWYYQIEILKL
EIGGQSLNLDCREYNADKAIVDSGTTLLRLPQKVFDAVVEAVARASLIPE
FSDGFWTGSQLACWTNTPWSYFPKISIYLRDENSSRSFRITILPQLYIQP
MECYRFGISPSTNALVIGATVMEGFYVIFDRAQKRVGFAASPCAEIAGAA
VSEISGPFSTEDVASNCVP
3D structure
PDB7d5b Structure-Based Approaches to Improving Selectivity through Utilizing Explicit Water Molecules: Discovery of Selective beta-Secretase (BACE1) Inhibitors over BACE2.
ChainA
Resolution1.31 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D48 S51 N53 A55 Y87 D241 T244
Catalytic site (residue number reindexed from 1) D36 S39 N41 A43 Y75 D222 T225
Enzyme Commision number 3.4.23.45: memapsin 1.
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 66F A S26 R28 G29 L46 D48 Y87 F124 D241 G243 T245 S14 R16 G17 L34 D36 Y75 F112 D222 G224 T226
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:7d5b, PDBe:7d5b, PDBj:7d5b
PDBsum7d5b
PubMed33719429
UniProtQ9Y5Z0|BACE2_HUMAN Beta-secretase 2 (Gene Name=BACE2)

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