6FGY

Crystal Structure of Human BACE-1 in Complex with amino-1,4-oxazine compound 4

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	14
Details	binding site for residue D9W A 501

Chain	Residue
A	GLY59
A	ASP276
A	SER277
A	GLY278
A	THR280
A	ALA383
A	GLN60
A	GLY61
A	LEU78
A	ASP80
A	TYR119
A	PHE156
A	ILE158
A	ILE166

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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	ILE77-VAL88

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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	ASP80
A	ASP276

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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	LYS113
A	LYS262
A	LYS266
A	LYS272
A	LYS286
A	LYS287
A	LYS294

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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	ASN140
A	ASN159
A	ASN210
A	ASN341

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