4I0Z

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

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004190	molecular_function	aspartic-type endopeptidase activity
A	0006508	biological_process	proteolysis
A	0016020	cellular_component	membrane

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE 1BB A 501

Chain	Residue
A	GLN73
A	THR292
A	THR293
A	ASN294
A	ARG296
A	SER386
A	HOH694
A	GLY74
A	LEU91
A	ASP93
A	TYR132
A	GLN134
A	GLY135
A	LYS168
A	GLY291

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site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN A 502

Chain	Residue
A	GLU78
A	HIS110
A	HIS150
A	HOH653
A	HOH717

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site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 503

Chain	Residue
A	GLU316
A	ASP451
A	HIS457
A	HIS459

---

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN A 504

Chain	Residue
A	ASP192
A	HIS458
A	HOH812

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site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ZN A 505

Chain	Residue
A	GLU165
A	ASP167

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Functional Information from PROSITE/UniProt

site_id	PS00141
Number of Residues	12
Details	ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ILVDTGSSNFAV

Chain	Residue	Details
A	ILE90-VAL101

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	7
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"17425515","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19011241","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	3
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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