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3UDJ

Crystal Structure of BACE with Compound 5

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
A0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 092 A 401
ChainResidue
ALEU30
AASP32
AGLY34
ATYR71
AGLN73
APHE108
AASP228
AGLY230
AHOH587

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 402
ChainResidue
AARG96
AASN98
AGLU134
AGLN143

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 403
ChainResidue
ALYS218
AHOH635

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PEG A 409
ChainResidue
AGLY11
AGLY13
ATYR14
ASER229
AGLY230
ATHR232
AALA335
AHOH534
AHOH583
AHOH633

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 404
ChainResidue
AGLU255
AASP390
AHIS396
AHIS398

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

246704

PDB entries from 2025-12-24

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