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3ZMG

CRYSTAL STRUCTURE OF BACE-1 IN COMPLEX WITH CHEMICAL LIGAND

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
A0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 6Z0 A 1448
ChainResidue
AGLY72
ATHR293
AALA396
AHOH2412
AGLY74
ALEU91
AASP93
ATYR132
APHE169
AASP289
ASER290
AGLY291

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 1449
ChainResidue
AHIS242
ATYR245
AHOH2240
AHOH2244
AHOH2245

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 1450
ChainResidue
AVAL202
ATHR205
AHOH2212
AHOH2213
AHOH2214
AHOH2218

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE DMS A 1451
ChainResidue
AARG157
AGLU195

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ILVDTGSSNFAV
ChainResidueDetails
AILE90-VAL101

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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