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4KE0

Crystal structure of BACE1 in complex with hydroxyethylamine-macrocyclic inhibitor 13

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
A0016020cellular_componentmembrane
B0004190molecular_functionaspartic-type endopeptidase activity
B0006508biological_processproteolysis
B0016020cellular_componentmembrane
C0004190molecular_functionaspartic-type endopeptidase activity
C0006508biological_processproteolysis
C0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 1R8 A 501
ChainResidue
AASP32
ATHR329
AHOH660
AGLY34
APRO70
ATYR71
ATHR72
APHE108
AILE110
AASP228
AGLY230

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 502
ChainResidue
AARG50
ATYR51
AGLN53

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 503
ChainResidue
AARG235
AGLN326
ASER327
ASER328
ATHR329

site_idAC4
Number of Residues14
DetailsBINDING SITE FOR RESIDUE 1R8 B 501
ChainResidue
BLEU30
BASP32
BGLY34
BSER35
BPRO70
BTYR71
BTHR72
BPHE108
BILE110
BASP228
BGLY230
BARG235
BTHR329
BHOH620

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 502
ChainResidue
BTHR292
BASP378
BHOH629
BHOH753

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 1R8 C 501
ChainResidue
CASP32
CGLY34
CPRO70
CTYR71
CTHR72
CPHE108
CTRP115
CASP228
CGLY230
CTHR329
CVAL332
CHOH699

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 Residues6
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues21
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 Residues9
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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