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3ZKI

BACE2 MUTANT STRUCTURE WITH LIGAND

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
A0016020cellular_componentmembrane
B0004190molecular_functionaspartic-type endopeptidase activity
B0006508biological_processproteolysis
B0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE WZV A 1398
ChainResidue
AGLY27
ASER242
AGLY243
ATHR244
ATHR245
AALA347
ATHR348
AGLU351
AHOH2005
AHOH2060
AARG28
AGLY29
ATYR30
ALEU46
AASP48
ATYR87
ATRP131
AASP241

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE WZV B 1398
ChainResidue
BGLY27
BARG28
BGLY29
BTYR30
BLEU46
BASP48
BTYR87
BTRP131
BASP241
BSER242
BGLY243
BTHR244
BTHR245
BALA347
BTHR348
BHOH2001
BHOH2019

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ILVDTGSSNFAV
ChainResidueDetails
AILE45-VAL56
AALA238-LEU249

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

251174

PDB entries from 2026-03-25

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