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3L5C

Structure of BACE Bound to SCH723871

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 Residues7
DetailsBINDING SITE FOR RESIDUE TAR A 2
ChainResidue
AARG68
AASN89
AHIS110
AARG111
AASN175
AHOH562
AHOH621

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE BDQ A 1
ChainResidue
ATYR132
ALYS168
APHE169
ATYR259
AILE287
AASP289
AGLY291
ATHR292
AHOH885
ALEU91
AASP93

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE TAR B 3
ChainResidue
BARG68
BASN89
BHIS110
BARG111
BASN175
BHOH524
BHOH589
BHOH679
BHOH686

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE BDQ B 1
ChainResidue
BLEU91
BASP93
BTYR132
BLYS168
BPHE169
BTYR259
BASP289
BGLY291

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

site_idSWS_FT_FI2
Number of Residues14
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 Residues8
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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