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6DHC

X-ray structure of BACE1 in complex with a bicyclic isoxazoline carboxamide as the P3 ligand

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 Residues19
Detailsbinding site for residue GHJ A 401
ChainResidue
AGLY11
AGLN73
APHE108
AILE110
AILE126
ATYR198
AASP228
AGLY230
ATHR231
ATHR232
AHOH545
AGLN12
AGLY13
ALEU30
AASP32
AGLY34
APRO70
ATYR71
ATHR72

site_idAC2
Number of Residues2
Detailsbinding site for residue GOL A 402
ChainResidue
AGLY372
AHOH542

site_idAC3
Number of Residues4
Detailsbinding site for residue GOL A 403
ChainResidue
ASER10
AGLY11
AGLN12
AVAL309

site_idAC4
Number of Residues3
Detailsbinding site for residue GOL A 404
ChainResidue
AASP4
AGLN153
ASER173

site_idAC5
Number of Residues3
Detailsbinding site for residue URE A 405
ChainResidue
ATHR185
AGLY186
CLYS65

site_idAC6
Number of Residues3
Detailsbinding site for residue URE A 406
ChainResidue
AGLU219
ATYR222
ALYS239

site_idAC7
Number of Residues3
Detailsbinding site for residue URE A 407
ChainResidue
AHIS89
AHOH526
CLYS107

site_idAC8
Number of Residues21
Detailsbinding site for residue GHJ B 401
ChainResidue
BGLY11
BGLN12
BGLY13
BLEU30
BASP32
BGLY34
BSER35
BPRO70
BTYR71
BTHR72
BGLN73
BPHE108
BILE110
BILE126
BTYR198
BASP228
BGLY230
BTHR231
BTHR232
BHOH521
BHOH526

site_idAC9
Number of Residues4
Detailsbinding site for residue GOL B 402
ChainResidue
BTYR286
BVAL375
BTHR376
CTHR292

site_idAD1
Number of Residues1
Detailsbinding site for residue GOL B 403
ChainResidue
BGLU290

site_idAD2
Number of Residues2
Detailsbinding site for residue GOL B 404
ChainResidue
BARG349
BARG351

site_idAD3
Number of Residues4
Detailsbinding site for residue URE B 405
ChainResidue
BTHR82
BARG96
BASN98
BGLU134

site_idAD4
Number of Residues18
Detailsbinding site for residue GHJ C 401
ChainResidue
CGLY11
CGLN12
CLEU30
CASP32
CGLY34
CSER35
CPRO70
CTYR71
CTHR72
CGLN73
CTYR198
CASP228
CGLY230
CTHR231
CTHR232
CARG235
CHOH536
CHOH540

site_idAD5
Number of Residues9
Detailsbinding site for residue GOL C 402
ChainResidue
CLYS9
CSER10
CGLY11
CGLN12
CGLY13
CTYR14
CVAL170
CTHR232
CGLU339

site_idAD6
Number of Residues4
Detailsbinding site for residue GOL C 403
ChainResidue
CMET215
CVAL204
CARG205
CASP212

site_idAD7
Number of Residues7
Detailsbinding site for residue GOL C 404
ChainResidue
CHIS45
CPHE47
CSER105
CASP106
CLYS107
CPHE108
CPHE109

site_idAD8
Number of Residues3
Detailsbinding site for residue SO4 C 405
ChainResidue
CARG349
CARG351
CHOH524

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 2024-07-17

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