Structure of PDB 3zki Chain A

Receptor sequence
>3zkiA (length=365) Species: 9606 (Homo sapiens) [Search protein sequence]
NFLAMVDNLQGDSGRGYYLEMLIGTPPQKLQILVDTGSSNFAVAGTPHSY
IDTYFDTERSSTYRSKGFDVTVKYTQGSWTGFVGEDLVTIPKGFNTSFLV
NIATIFESENFFLPGIKWNGILGLAYATLAKPSSSLETFFDSLVTQANIP
NVFSMQMCGAGNGGSLVLGGIEPSLYKGDIWYTPIKEEWYYQIEILKLEI
GGQSLNLDCREYNADKAIVDSGTTLLRLPQKVFDAVVEAVARASLIFSDG
FWTGSQLACWTPWSYFPKISIYLRDENSSRSFRITILPQLYIQPMMYECY
RFGISPSTNALVIGATVMEGFYVIFDRAQKRVGFAASPCAEIAGAAVSEI
SGPFSTEDVASNCVP
3D structure
PDB3zki Mapping the Conformational Space Accessible to Bace2 Using Surface Mutants and Co-Crystals with Fab-Fragments, Fynomers, and Xaperones
ChainA
Resolution2.4 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) D35 S38 N40 A42 Y74 D220 T223
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 WZV A G27 R28 G29 L46 D48 Y87 W131 I134 D241 G243 T244 T245 A347 G14 R15 G16 L33 D35 Y74 W118 I121 D220 G222 T223 T224 A315 PDBbind-CN: -logKd/Ki=5.92,IC50=1.2uM
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:3zki, PDBe:3zki, PDBj:3zki
PDBsum3zki
PubMed23695257
UniProtQ9Y5Z0|BACE2_HUMAN Beta-secretase 2 (Gene Name=BACE2)

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