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5QDC

Crystal structure of BACE complex with BMC019 hydrolyzed

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 Residues6
Detailsbinding site for residue GOL A 401
ChainResidue
AGLY34
APRO70
AILE126
AARG128
ATYR198
AE77402

site_idAC2
Number of Residues17
Detailsbinding site for residue E77 A 402
ChainResidue
ALEU30
AASP32
ATYR71
ATHR72
AGLN73
APHE108
AILE110
ATRP115
AASP228
AGLY230
ATHR232
AARG235
AGOL401
AHOH589
AGLY11
AGLN12
AGLY13

site_idAC3
Number of Residues7
Detailsbinding site for residue GOL B 401
ChainResidue
BGLY34
BPRO70
BTYR71
BILE126
BARG128
BTYR198
BE77402

site_idAC4
Number of Residues15
Detailsbinding site for residue E77 B 402
ChainResidue
BGLY11
BGLN12
BGLY13
BLEU30
BASP32
BTYR71
BTHR72
BGLN73
BPHE108
BTRP115
BASP228
BGLY230
BTHR232
BARG235
BGOL401

site_idAC5
Number of Residues6
Detailsbinding site for residue GOL C 401
ChainResidue
CGLY34
CVAL69
CPRO70
CILE126
CARG128
CE77402

site_idAC6
Number of Residues16
Detailsbinding site for residue E77 C 402
ChainResidue
CGLY11
CGLN12
CGLY13
CLEU30
CASP32
CTYR71
CTHR72
CGLN73
CPHE108
CILE110
CTRP115
CASP228
CGLY230
CTHR232
CARG235
CGOL401

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
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094
ChainResidueDetails
AASP32
AASP228
BASP32
BASP228
CASP32
CASP228

site_idSWS_FT_FI2
Number of Residues21
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241
ChainResidueDetails
ALYS65
BLYS218
BLYS224
BLYS238
BLYS239
BLYS246
CLYS65
CLYS214
CLYS218
CLYS224
CLYS238
ALYS214
CLYS239
CLYS246
ALYS218
ALYS224
ALYS238
ALYS239
ALYS246
BLYS65
BLYS214

site_idSWS_FT_FI3
Number of Residues12
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN92
CASN111
CASN162
CASN293
AASN111
AASN162
AASN293
BASN92
BASN111
BASN162
BASN293
CASN92

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PDB entries from 2024-07-24

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