6PZ4

co-crystal structure of BACE with inhibitor AM-6494

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	1
Details	binding site for residue IOD A 501

Chain	Residue
A	SER166

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site_id	AC2
Number of Residues	1
Details	binding site for residue IOD A 502

Chain	Residue
A	LYS168

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site_id	AC3
Number of Residues	2
Details	binding site for residue IOD A 503

Chain	Residue
A	HOH876
A	HOH876

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site_id	AC4
Number of Residues	8
Details	binding site for residue GOL A 504

Chain	Residue
A	HOH645
A	HOH810
A	HOH815
A	ARG111
A	TYR112
A	GLN114
A	SER248
A	HOH611

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site_id	AC5
Number of Residues	5
Details	binding site for residue GOL A 505

Chain	Residue
A	GLY127
A	TYR129
A	CYS330
A	THR375
A	HOH602

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site_id	AC6
Number of Residues	16
Details	binding site for residue P6J A 506

Chain	Residue
A	LYS70
A	GLY72
A	GLN73
A	GLY74
A	TYR75
A	ASP93
A	GLY95
A	TYR132
A	LYS168
A	PHE169
A	ASP289
A	SER290
A	GLY291
A	THR293
A	ALA396
A	HOH782

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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	ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094

Chain	Residue	Details
A	ASP93
A	ASP289

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site_id	SWS_FT_FI2
Number of Residues	7
Details	MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241

Chain	Residue	Details
A	LYS126
A	LYS275
A	LYS279
A	LYS285
A	LYS299
A	LYS300
A	LYS307

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site_id	SWS_FT_FI3
Number of Residues	4
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN153
A	ASN172
A	ASN223
A	ASN354

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