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4ZSP

BACE crystal structure with bicyclic aminothiazine 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 Residues13
Detailsbinding site for residue 4RZ A 401
ChainResidue
ASER10
ASER229
AGLY230
ATHR232
AHOH618
AGLY11
AGLN12
AGLY13
AASP32
AGLY34
ATYR71
ATRP115
AASP228

site_idAC2
Number of Residues8
Detailsbinding site for residue GOL A 402
ChainResidue
AASP318
AHOH513
AHOH567
AHOH729
BSER58
BTHR59
BARG61
BARG96

site_idAC3
Number of Residues13
Detailsbinding site for residue 4RZ B 401
ChainResidue
BSER10
BGLY11
BGLN12
BGLY13
BASP32
BGLY34
BTYR71
BTRP115
BASP228
BSER229
BGLY230
BTHR232
BHOH544

site_idAC4
Number of Residues8
Detailsbinding site for residue GOL B 402
ChainResidue
ASER58
ATHR59
AARG61
AARG96
BASP318
BHOH528
BHOH596
BHOH635

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 2025-06-11

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