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4DV9

Crystal structure of BACE1 with its inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
A0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 401
ChainResidue
AARG50
ATYR51
AGLN53

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 402
ChainResidue
ATYR51
AGLN53
AGLN55
ALYS218
AHOH725

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 403
ChainResidue
AGLU134
ASER139
AGLN143
AHOH679
AARG96

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 404
ChainResidue
ASER22
APRO23
ASER58
AHIS145
APRO147
AHOH554

site_idAC5
Number of Residues26
DetailsBINDING SITE FOR CHAIN B OF 8-MER PEPTIDE INHIBITOR
ChainResidue
AGLY11
ALEU30
AASP32
AGLY34
AVAL69
APRO70
ATYR71
ATHR72
AGLN73
APHE108
AILE110
AILE126
ALEU188
ATYR190
ATRP197
ATYR198
AASP228
AGLY230
ATHR231
ATHR232
AARG235
AHOH547
AHOH581
AHOH593
AHOH680
BHOH101

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 Residues2
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues7
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 Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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