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3L58

Structure of BACE Bound to SCH589432

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
A0016020cellular_componentmembrane
B0004190molecular_functionaspartic-type endopeptidase activity
B0006508biological_processproteolysis
B0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE CS5 A 1
ChainResidue
AGLY72
APHE169
AILE171
ATRP176
ATYR259
AASP289
AGLY291
ATHR292
ATHR293
AARG296
AHOH968
ALEU91
AASP93
AGLY95
APRO131
ATYR132
ATHR133
AGLN134
AGLY135

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE CS5 B 1
ChainResidue
BGLY72
BLEU91
BASP93
BGLY95
BSER96
BPRO131
BTYR132
BTHR133
BGLN134
BGLY135
BPHE169
BILE171
BTRP176
BTYR259
BASP289
BGLY291
BTHR292
BTHR293
BARG296
BHOH916

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 Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094
ChainResidueDetails
AASP93
AASP289
BASP93
BASP289

site_idSWS_FT_FI2
Number of Residues14
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241
ChainResidueDetails
ALYS126
BLYS279
BLYS285
BLYS299
BLYS300
BLYS307
ALYS275
ALYS279
ALYS285
ALYS299
ALYS300
ALYS307
BLYS126
BLYS275

site_idSWS_FT_FI3
Number of Residues8
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN153
AASN172
AASN223
AASN354
BASN153
BASN172
BASN223
BASN354

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PDB entries from 2024-11-06

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