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3KN0

Structure of BACE bound to SCH708236

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 Residues11
DetailsBINDING SITE FOR RESIDUE 3TO A 501
ChainResidue
ASER71
ATHR292
ATHR293
AGLN73
AGLY74
AASP93
ATYR132
AILE179
AASP289
ASER290
AGLY291

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE TLA A 502
ChainResidue
AARG68
AASN89
AHIS110
AARG111
AASN175
AHOH554
AHOH612
AHOH627

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 3TO B 501
ChainResidue
BSER71
BGLN73
BGLY74
BASP93
BGLY95
BTYR132
BGLN134
BILE179
BASP289
BSER290
BGLY291
BTHR292
BTHR293

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE TLA B 502
ChainResidue
BARG68
BASN89
BHIS110
BARG111
BASN175
BHOH507
BHOH572
BHOH662

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 2024-05-01

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