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3N4L

BACE-1 in complex with ELN380842

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
A0016020cellular_componentmembrane
B0004190molecular_functionaspartic-type endopeptidase activity
B0006508biological_processproteolysis
B0016020cellular_componentmembrane
C0004190molecular_functionaspartic-type endopeptidase activity
C0006508biological_processproteolysis
C0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 842 A 407
ChainResidue
AASP38
AASP234
AGLY236
AGLY40
APRO76
ATYR77
ATHR78
APHE114
AILE132
ATYR204
AILE232

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE 842 B 407
ChainResidue
BLEU36
BASP38
BGLY40
BPRO76
BTYR77
BTHR78
BPHE114
BTRP121
BILE132
BTYR204
BILE232
BASP234
BGLY236
BTHR237

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE 842 C 407
ChainResidue
CLEU36
CASP38
CGLY40
CPRO76
CTYR77
CTHR78
CPHE114
CTRP121
CILE124
CILE132
CTYR204
CASP234
CGLY236
CTHR237

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ILVDTGSSNFAV
ChainResidueDetails
AILE35-VAL46

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues21
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"17425515","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19011241","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues9
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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