Structure of PDB 3zki Chain B

Receptor sequence
>3zkiB (length=361) Species: 9606 (Homo sapiens) [Search protein sequence]
LAMVDNLQGDSGRGYYLEMLIGTPPQKLQILVDTGSSNFAVAGTPHSYID
TYFDTERSSTYRSKGFDVTVKYTQGSWTGFVGEDLVTIPKGFNTSFLVNI
ATIFESENFFLPGIKWNGILGLAYATLAKPSSSLETFFDSLVTQANIPNV
FSMQMCGANGGSLVLGGIEPSLYKGDIWYTPIKEEWYYQIEILKLEIGGQ
SLNLDCREYNADKAIVDSGTTLLRLPQKVFDAVVEAVARASSDGFWTGSQ
LACWTTPWSYFPKISIYLRDENSSRSFRITILPQLYIQPMMGYECYRFGI
SPSTNALVIGATVMEGFYVIFDRAQKRVGFAASPCAEIAGAAVSEISGPF
STEDVASNCVP
3D structure
PDB3zki Mapping the Conformational Space Accessible to Bace2 Using Surface Mutants and Co-Crystals with Fab-Fragments, Fynomers, and Xaperones
ChainB
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) D33 S36 N38 A40 Y72 D217 T220
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 B G27 G29 L46 D48 Y87 W131 D241 G243 T245 A347 G12 G14 L31 D33 Y72 W116 D217 G219 T221 A311
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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