Structure of PDB 3zkn Chain B

Receptor sequence
>3zknB (length=375) Species: 9606 (Homo sapiens) [Search protein sequence]
NFLAMVDNLQGDSGRGYYLEMLIGTPPQKLQILVDTGSSNFAVAGTPHSY
IDTYFDTERSSTYRSKGFDVTVKYTQGSWTGFVGEDLVTIPKGFNTSFLV
NIATIFESENFFLPGIKWNGILGLAYATLAKPSSSLETFFDSLVTQANIP
NVFSMQMCGANGGSLVLGGIEPSLYKGDIWYTPIKEEWYYQIEILKLEIG
GQSLNLDCREYNADKAIVDSGTTLLRLPQKVFDAVVEAVARASLIPEFSD
GFWTGSQLACWTNSETPWSYFPKISIYLRDENSSRSFRITILPQLYIQPM
MGAGLNYECYRFGISPSTNALVIGATVMEGFYVIFDRAQKRVGFAASPCA
EIAGAAVSEISGPFSTEDVASNCVP
3D structure
PDB3zkn Mapping the Conformational Space Accessible to Bace2 Using Surface Mutants and Co-Crystals with Fab-Fragments, Fynomers, and Xaperones
ChainB
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 D219 T222
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 D48 Y87 Q89 N123 L126 I134 D241 D35 Y74 Q76 N110 L113 I121 D219
Gene Ontology
Molecular Function
GO:0004190 aspartic-type endopeptidase activity
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0016020 membrane

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3zkn, PDBe:3zkn, PDBj:3zkn
PDBsum3zkn
PubMed23695257
UniProtQ9Y5Z0|BACE2_HUMAN Beta-secretase 2 (Gene Name=BACE2)

[Back to BioLiP]