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4TRZ

Structure of BACE1 complex with 2-thiophenyl 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 Residues18
DetailsBINDING SITE FOR CHAIN D OF 2-THIOPHENYL HEA-TYPE INHIBITOR
ChainResidue
ASER71
AILE171
ATRP176
AILE179
ATYR259
AASP289
AGLY291
ATHR292
ATHR293
AASN294
AGLY72
AGLN73
AGLY74
AASP93
AGLY95
ATYR132
AGLN134
APHE169

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR CHAIN E OF 2-THIOPHENYL HEA-TYPE INHIBITOR
ChainResidue
BGLY72
BGLN73
BGLY74
BASP93
BGLY95
BTYR132
BTHR133
BGLN134
BPHE169
BILE179
BTYR259
BILE287
BASP289
BGLY291
BTHR292
BTHR293
BASN294
BARG296

site_idAC3
Number of Residues20
DetailsBINDING SITE FOR CHAIN F OF 2-THIOPHENYL HEA-TYPE INHIBITOR
ChainResidue
CGLY72
CGLY74
CLEU91
CASP93
CTYR132
CTHR133
CGLN134
CPHE169
CILE171
CILE179
CTYR259
CILE287
CASP289
CGLY291
CTHR292
CTHR293
CASN294
CARG296
CARG368
FHOH101

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 Residues1023
DetailsDomain: {"description":"Peptidase A1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01103","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
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_FI4
Number of Residues12
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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