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4LXA

Crystal Structure of Human Beta Secretase in Complex with Compound 11a

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 Residues21
DetailsBINDING SITE FOR RESIDUE 1YS A 501
ChainResidue
AGLY11
ATYR71
ATHR72
AGLY74
APHE108
AILE110
AILE126
AASP228
AGLY230
ATHR231
ATHR232
AGLN12
AHOH619
AHOH702
AGLY13
ALEU30
AASP32
AGLY34
ASER35
AVAL69
APRO70

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 501
ChainResidue
BARG205
BVAL375
BTHR376
BHOH745

site_idAC3
Number of Residues21
DetailsBINDING SITE FOR RESIDUE 1YS B 502
ChainResidue
BGLY11
BGLN12
BGLY13
BLEU30
BASP32
BGLY34
BSER35
BVAL69
BPRO70
BTYR71
BTHR72
BPHE108
BASP228
BGLY230
BTHR231
BTHR232
BHOH626
BHOH685
BHOH686
BHOH727
BHOH763

site_idAC4
Number of Residues22
DetailsBINDING SITE FOR RESIDUE 1YS C 501
ChainResidue
CGLY11
CGLN12
CGLY13
CLEU30
CASP32
CGLY34
CSER35
CVAL69
CPRO70
CTYR71
CTHR72
CGLN73
CPHE108
CILE126
CASP228
CGLY230
CTHR231
CTHR232
CHOH612
CHOH617
CHOH701
CHOH703

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 C 502
ChainResidue
CGLU290
CARG349
CARG351
CHOH720

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

223532

PDB entries from 2024-08-07

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