2VIJ

Human BACE-1 in complex with 3-(1,1-dioxidotetrahydro-2H-1,2-thiazin- 2-yl)-5-(ethylamino)-N-((1S,2R)-2-hydroxy-1-(phenylmethyl)-3-(1,2,3,4- tetrahydro-1-naphthalenylamino)propyl)benzamide

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	19
Details	BINDING SITE FOR RESIDUE C44 A3000

Chain	Residue
A	GLY72
A	THR133
A	GLN134
A	PHE169
A	ASP289
A	GLY291
A	THR292
A	THR293
A	ASN294
A	ARG296
A	SER386
A	GLN73
A	GLY74
A	LEU91
A	ASP93
A	GLY95
A	SER96
A	PRO131
A	TYR132

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site_id	AC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE C44 A3001

Chain	Residue
A	LEU145
A	THR155
A	ASN270
A	GLY271
A	ASN339
A	VAL343
A	ALA374
A	PHE426
A	ARG427
A	THR428
A	HOH2311
A	HOH2359
A	HOH2379

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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	GLN153
A	GLN172
A	GLN223
A	GLN354

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