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3L5B

Structure of BACE Bound to SCH713601

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 Residues9
DetailsBINDING SITE FOR RESIDUE TAR A 2
ChainResidue
AARG68
AASN89
AHIS110
AARG111
AASN175
AHOH562
AHOH621
AHOH635
AHOH824

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE BDO A 1
ChainResidue
ALEU91
AASP93
AASP289
AGLY291
ATHR292
AHOH906

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE TAR B 1
ChainResidue
BHIS106
BPHE108
BSER166
BASP167
BLYS168
BPHE169
BPHE170
BHOH652
BHOH675

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE TAR B 3
ChainResidue
BARG68
BASN89
BHIS110
BARG111
BASN175
BHOH521
BHOH585
BHOH680

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE BDO B 455
ChainResidue
BLEU91
BASP93
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

246704

PDB entries from 2025-12-24

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