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4I11

Structure-based design of novel dihydroisoquinoline BACE-1 inhibitors that do not engage the catalytic aspartates.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
A0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 501
ChainResidue
AGLU316
AASP451
AHIS457
AHIS459

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 502
ChainResidue
AASP192
AHIS458
AHIS460
AHOH769

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 503
ChainResidue
AHIS110
AHIS150
AHOH755
AGLU78

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 1CH A 504
ChainResidue
AGLY72
AGLN73
AGLY74
ALEU91
ATYR132
AGLY291
ATHR292
ATHR293
AHOH850

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ILVDTGSSNFAV
ChainResidueDetails
AILE90-VAL101

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094
ChainResidueDetails
AASP93
AASP289

site_idSWS_FT_FI2
Number of Residues7
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241
ChainResidueDetails
ALYS126
ALYS275
ALYS279
ALYS285
ALYS299
ALYS300
ALYS307

site_idSWS_FT_FI3
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN153
AASN172
AASN223
AASN354

224004

PDB entries from 2024-08-21

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