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6UJ1

BACE2 mutant in complex with a macrocyclic compound

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 Residues16
Detailsbinding site for residue L3M A 401
ChainResidue
AASP48
AASP241
AGLY243
ATHR244
ATHR245
ALEU246
AARG248
ASER337
AGLY50
ALYS86
ATYR87
ATHR88
AGLN89
APHE124
ATYR211
AILE239

site_idAC2
Number of Residues18
Detailsbinding site for residue L3M B 401
ChainResidue
BLEU46
BASP48
BGLY50
BSER51
BTYR87
BTHR88
BGLN89
BPHE124
BTRP131
BTYR211
BILE239
BASP241
BGLY243
BTHR244
BTHR245
BLEU246
BARG248
BSER337

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

246031

PDB entries from 2025-12-10

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