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3UQP

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 Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 501
ChainResidue
AARG96
AASN98
AGLU134
ASER139
AGLN143
AHOH630

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 502
ChainResidue
AHIS145
APRO147
AHOH636
AHOH888
AHOH949
ASER22
APRO23
ASER58

site_idAC3
Number of Residues28
DetailsBINDING SITE FOR CHAIN B OF 8-MER PEPTIDE INHIBITOR
ChainResidue
AGLY11
AGLN12
AASP32
AGLY34
AVAL69
APRO70
ATYR71
ATHR72
AGLN73
APHE108
AILE110
ATRP115
AILE126
AARG128
ALEU188
ATRP197
ATYR198
AASP228
AGLY230
ATHR231
ATHR232
AASN233
AARG235
AHOH688
AHOH718
AHOH744
BHOH101
BHOH102

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

250835

PDB entries from 2026-03-18

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