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3HVG

Structure of bace (beta secretase) in Complex with EV0

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 Residues7
DetailsBINDING SITE FOR RESIDUE EV0 A 441
ChainResidue
AASP32
ATYR71
ATHR72
AGLN73
APHE108
ATRP115
AASP228

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EV0 B 441
ChainResidue
BASP32
BASP228

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EV0 B 442
ChainResidue
BLYS218
BGLU219
BTYR222
BTYR384

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL C 441
ChainResidue
CLYS9
CGLY11
CGLY13
CTYR14
CTHR232
CGLU339

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

221051

PDB entries from 2024-06-12

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