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4DVF

Crystal structure of BACE1 with its 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 Residues32
DetailsBINDING SITE FOR CHAIN C OF 7-MER PEPTIDE INHIBITOR
ChainResidue
AGLY11
AGLN73
APHE108
ATRP115
AILE126
ATRP197
ATYR198
ALYS224
AASP228
ASER229
AGLY230
AGLN12
ATHR231
ATHR232
AASN233
AARG235
AALA250
ASER253
ASER325
AALA335
AHOH504
AHOH660
AGLY13
CHOH101
CHOH102
CHOH103
ALEU30
AASP32
AGLY34
APRO70
ATYR71
ATHR72

site_idAC2
Number of Residues32
DetailsBINDING SITE FOR CHAIN D OF 7-MER PEPTIDE INHIBITOR
ChainResidue
BGLY11
BGLN12
BGLY13
BLEU30
BASP32
BGLY34
BPRO70
BTYR71
BTHR72
BGLN73
BTRP115
BILE118
BILE126
BARG128
BTRP197
BTYR198
BASP223
BLYS224
BASP228
BSER229
BGLY230
BTHR231
BTHR232
BASN233
BARG235
BARG307
BSER325
BALA335
DHOH101
DHOH102
DHOH103
DHOH104

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
AASP32
AASP228
BASP32
BASP228

site_idSWS_FT_FI2
Number of Residues14
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241
ChainResidueDetails
ALYS65
BLYS218
BLYS224
BLYS238
BLYS239
BLYS246
ALYS214
ALYS218
ALYS224
ALYS238
ALYS239
ALYS246
BLYS65
BLYS214

site_idSWS_FT_FI3
Number of Residues8
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN92
AASN111
AASN162
AASN293
BASN92
BASN111
BASN162
BASN293

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PDB entries from 2024-08-07

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