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4TRW

Structure of BACE1 complex with a syn-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 Residues14
DetailsBINDING SITE FOR CHAIN D OF L-ALPHA-GLUTAMYL-L-ISOLEUCYL-N-[(2R,3S)-1-{[(1S)-1- CARBOXYBUTYL]AMINO}-2-HYDROXY-5-METHYLHEXAN-3-YL]-3-THIOPHEN-2-YL-L- ALANINAMIDE
ChainResidue
AGLY72
AASP289
AGLY291
ATHR292
ATHR293
AASN294
AGLY74
AASP93
AGLY95
ATYR132
ATHR133
AGLN134
AILE171
ATYR259

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR CHAIN E OF L-ALPHA-GLUTAMYL-L-ISOLEUCYL-N-[(2R,3S)-1-{[(1S)-1- CARBOXYBUTYL]AMINO}-2-HYDROXY-5-METHYLHEXAN-3-YL]-3-THIOPHEN-2-YL-L- ALANINAMIDE
ChainResidue
BGLY72
BASP93
BGLY95
BPRO131
BTYR132
BTHR133
BGLN134
BPHE169
BTYR259
BASP289
BGLY291
BTHR292
BTHR293
BASN294

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR CHAIN F OF L-ALPHA-GLUTAMYL-L-ISOLEUCYL-N-[(2R,3S)-1-{[(1S)-1- CARBOXYBUTYL]AMINO}-2-HYDROXY-5-METHYLHEXAN-3-YL]-3-THIOPHEN-2-YL-L- ALANINAMIDE
ChainResidue
CGLY72
CLEU91
CASP93
CGLY95
CSER96
CPRO131
CTYR132
CTHR133
CGLN134
CTYR259
CASP289
CGLY291
CTHR292
CTHR293
CASN294
CARG296
CARG368
CLYS382

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 2024-06-26

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