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1FKN

Structure of Beta-Secretase Complexed with 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
Functional Information from PDB Data
site_idAC1
Number of Residues25
DetailsBINDING SITE FOR CHAIN C OF INHIBITOR
ChainResidue
ASER10
APHE108
AILE110
ATYR198
ALYS224
AASP228
AGLY230
ATHR231
ATHR232
AARG235
ATHR329
AGLY11
AHOH490
CHOH9
CHOH10
CHOH11
CHOH12
CHOH13
AASP32
AGLY34
ASER35
APRO70
ATYR71
ATHR72
AGLN73

site_idAC2
Number of Residues27
DetailsBINDING SITE FOR CHAIN D OF INHIBITOR
ChainResidue
BSER10
BGLY11
BASP32
BGLY34
BSER35
BPRO70
BTYR71
BTHR72
BGLN73
BPHE108
BTYR198
BASP228
BGLY230
BTHR231
BTHR232
BARG235
BSER328
BHOH440
BHOH449
BHOH498
BHOH566
BHOH583
DHOH9
DHOH10
DHOH11
DHOH13
DHOH14

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ILVDTGSSNFAV
ChainResidueDetails
AILE29-VAL40

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094
ChainResidueDetails
AALA42
ALYS238
BALA42
BLYS238

site_idSWS_FT_FI2
Number of Residues14
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241
ChainResidueDetails
ALYS75
BASP228
BLEU234
BILE248
BLYS249
BLYS256
ALYS224
AASP228
ALEU234
AILE248
ALYS249
ALYS256
BLYS75
BLYS224

site_idSWS_FT_FI3
Number of Residues8
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AILE102
ALEU121
AGLY172
AGLN303
BILE102
BLEU121
BGLY172
BGLN303

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
ATHR231
AASP228
ASER35
AASP32

site_idCSA10
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
BTHR231
BASP228
BASP32
BTHR33

site_idCSA11
Number of Residues2
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
AASP228
AASP32

site_idCSA12
Number of Residues2
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
BASP228
BASP32

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
BTHR231
BASP228
BSER35
BASP32

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
AASP228
ASER229
AASP32
ATHR33

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
BASP228
BSER229
BASP32
BTHR33

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
AASP228
ASER35
AASP32

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
BASP228
BSER35
BASP32

site_idCSA7
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
AASP228
ASER35
ATYR71
AASP32

site_idCSA8
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
BASP228
BSER35
BTYR71
BASP32

site_idCSA9
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
ATHR231
AASP228
AASP32
ATHR33

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PDB entries from 2024-07-31

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