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5QD0

Crystal structure of BACE complex withBMC006

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 Residues15
Detailsbinding site for residue E5Y A 401
ChainResidue
AGLY11
AILE126
AASP228
AGLY230
ATHR231
ATHR232
AHOH515
ALEU30
AASP32
AGLY34
AVAL69
APRO70
ATYR71
ATHR72
AGLN73

site_idAC2
Number of Residues15
Detailsbinding site for residue E5Y B 401
ChainResidue
BLEU30
BASP32
BGLY34
BPRO70
BTYR71
BTHR72
BGLN73
BTRP115
BILE126
BARG128
BTYR198
BASP228
BGLY230
BTHR231
BTHR232

site_idAC3
Number of Residues13
Detailsbinding site for residue E5Y C 401
ChainResidue
CLEU30
CASP32
CGLY34
CSER35
CTYR71
CTHR72
CGLN73
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

240971

PDB entries from 2025-08-27

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