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2F3E

Crystal Structure of the Bace complex with AXQ093, a macrocyclic inhibitor

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 AXQ A 601
ChainResidue
AGLY11
AGLN73
AILE110
ATRP115
ATYR198
AASP228
AGLY230
ATHR231
ATHR232
AARG307
AHOH655
AGLN12
AGLY13
ALEU30
AASP32
AGLY34
APRO70
ATYR71
ATHR72

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE AXQ B 602
ChainResidue
BGLY11
BGLN12
BGLY13
BLEU30
BASP32
BGLY34
BPRO70
BTYR71
BTHR72
BGLN73
BILE110
BTRP115
BTYR198
BASP228
BGLY230
BTHR231
BTHR232
BARG307
BHOH691

site_idAC3
Number of Residues20
DetailsBINDING SITE FOR RESIDUE AXQ C 603
ChainResidue
CGLY11
CGLN12
CGLY13
CLEU30
CASP32
CGLY34
CPRO70
CTYR71
CTHR72
CGLN73
CILE110
CTRP115
CTYR198
CASP228
CGLY230
CTHR231
CTHR232
CARG307
CHOH628
CHOH695

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
ALYS214
ALYS218
ALYS224
ALYS238
ALYS239
ALYS246
BLYS65
BLYS214
BLYS218
BLYS224
BLYS238
BLYS239
BLYS246
CLYS65
CLYS214
CLYS218
CLYS224
CLYS238
CLYS239
CLYS246

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

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PDB entries from 2024-05-29

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