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4TRY

Structure of BACE1 complex with a HEA-type inhibitor

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 "syn-HEA type inhibitor
ChainResidue
BGLY72
BASP289
BGLY291
BTHR292
BTHR293
BASN294
BARG296
EHOH101
BGLN73
BASP93
BTYR132
BTHR133
BGLN134
BPHE169
BILE171
BTYR259

site_idAC2
Number of Residues16
Detailsbinding site for "syn-HEA type inhibitor
ChainResidue
BGLY72
BGLN73
BASP93
BTYR132
BTHR133
BGLN134
BPHE169
BILE171
BTYR259
BASP289
BGLY291
BTHR292
BTHR293
BASN294
BARG296
EHOH101

site_idAC3
Number of Residues16
Detailsbinding site for "syn-HEA type inhibitor
ChainResidue
BGLY72
BGLN73
BASP93
BTYR132
BTHR133
BGLN134
BPHE169
BILE171
BTYR259
BASP289
BGLY291
BTHR292
BTHR293
BASN294
BARG296
EHOH101

site_idAC4
Number of Residues16
Detailsbinding site for "syn-HEA type inhibitor
ChainResidue
BGLY72
BGLN73
BASP93
BTYR132
BTHR133
BGLN134
BPHE169
BILE171
BTYR259
BASP289
BGLY291
BTHR292
BTHR293
BASN294
BARG296
EHOH101

site_idAC5
Number of Residues16
Detailsbinding site for "syn-HEA type inhibitor
ChainResidue
BGLY72
BGLN73
BASP93
BTYR132
BTHR133
BGLN134
BPHE169
BILE171
BTYR259
BASP289
BGLY291
BTHR292
BTHR293
BASN294
BARG296
EHOH101

site_idAC6
Number of Residues16
Detailsbinding site for "syn-HEA type inhibitor
ChainResidue
BGLY72
BGLN73
BASP93
BTYR132
BTHR133
BGLN134
BPHE169
BILE171
BTYR259
BASP289
BGLY291
BTHR292
BTHR293
BASN294
BARG296
EHOH101

site_idAC7
Number of Residues16
Details
ChainResidue
CTYR132
CTHR133
CGLN134
CPHE169
CILE171
CTYR259
CASP289
CGLY291
CTHR292
CTHR293
CASN294
CARG296
FHOH101
CSER71
CGLY72
CASP93

site_idAC8
Number of Residues15
Details
ChainResidue
AGLY72
AGLN73
AGLY74
AASP93
ATYR132
ATHR133
AGLN134
APHE169
ATYR259
AILE287
AASP289
AGLY291
ATHR292
ATHR293
AASN294

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ILVDTGSSNFAV
ChainResidueDetails
AILE90-VAL101

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094
ChainResidueDetails
AASP93
AASP289
BASP93
BASP289
CASP93
CASP289

site_idSWS_FT_FI2
Number of Residues21
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241
ChainResidueDetails
ALYS126
BLYS279
BLYS285
BLYS299
BLYS300
BLYS307
CLYS126
CLYS275
CLYS279
CLYS285
CLYS299
ALYS275
CLYS300
CLYS307
ALYS279
ALYS285
ALYS299
ALYS300
ALYS307
BLYS126
BLYS275

site_idSWS_FT_FI3
Number of Residues12
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN153
CASN172
CASN223
CASN354
AASN172
AASN223
AASN354
BASN153
BASN172
BASN223
BASN354
CASN153

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PDB entries from 2024-04-24

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