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3K5F

Human BACE-1 COMPLEX WITH AYH011

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 Residues16
DetailsBINDING SITE FOR RESIDUE AYH A 387
ChainResidue
AGLN12
AILE126
ATYR198
AASP228
AGLY230
ATHR231
ATHR232
AHOH419
AGLY13
AASP32
AGLY34
APRO70
ATYR71
ATHR72
AGLN73
APHE108

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE AYH B 387
ChainResidue
BGLN12
BGLY13
BASP32
BGLY34
BPRO70
BTYR71
BTHR72
BGLN73
BPHE108
BILE126
BTYR198
BASP228
BGLY230
BTHR232
BHOH477

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE AYH C 387
ChainResidue
CGLN12
CGLY13
CASP32
CGLY34
CPRO70
CTYR71
CTHR72
CGLN73
CPHE108
CILE126
CTYR198
CASP228
CGLY230
CTHR231
CTHR232

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ILVDTGSSNFAV
ChainResidueDetails
AILE29-VAL40

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

242500

PDB entries from 2025-10-01

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