5MCQ

CRYSTAL STRUCTURE OF BACE-1 IN COMPLEX WITH ACTIVE SITE AND EXOSITE BINDING PEPTIDE INHIBITOR

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	4
Details	binding site for residue EDO A 501

Chain	Residue
A	ARG111
A	TYR112
A	GLN114
A	HOH851

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site_id	AC2
Number of Residues	5
Details	binding site for residue EDO A 502

Chain	Residue
A	SER59
A	PHE60
A	GLU165
A	HOH975
A	HOH1005

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site_id	AC3
Number of Residues	5
Details	binding site for residue EDO A 503

Chain	Residue
A	ARG157
A	ASN159
A	GLU195
A	SER200
A	HOH729

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site_id	AC4
Number of Residues	2
Details	binding site for residue EDO A 504

Chain	Residue
A	GLU226
A	HOH844

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site_id	AC5
Number of Residues	14
Details	binding site for Ligand residues STA D 671 through VAL D 672 bound to ASN D 670

Chain	Residue
A	ASP93
A	GLY95
A	SER96
A	PRO131
A	TYR132
A	THR133
A	GLN134
A	ILE187
A	TYR259
A	ASP289
A	GLY291
D	ASN670
D	ALA673
D	GLU674

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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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