3R2F

Crystal structure of beta-site app-cleaving enzyme 1 (BACE-WT) complex with BMS-693391 AKA (2S)-2-((3R)-3-acetamido-3-isobutyl-2-oxo-1-pyrrolidinyl)-N-((1S,2R)-1-(3,5-difluorobenzyl)-2-hydroxy-2-((2R,4R)-4-propoxy-2-pyrrolidinyl)ethyl)-4-phenylbutanamide

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
B	0004190	molecular_function	aspartic-type endopeptidase activity
B	0006508	biological_process	proteolysis
B	0016020	cellular_component	membrane
D	0004190	molecular_function	aspartic-type endopeptidase activity
D	0006508	biological_process	proteolysis
D	0016020	cellular_component	membrane
E	0004190	molecular_function	aspartic-type endopeptidase activity
E	0006508	biological_process	proteolysis
E	0016020	cellular_component	membrane

Functional Information from PDB Data

site_id	AC1
Number of Residues	19
Details	BINDING SITE FOR RESIDUE PB0 A 394

Chain	Residue
A	GLY11
A	PHE108
A	ILE110
A	TRP115
A	TYR198
A	ASP228
A	GLY230
A	THR231
A	THR232
A	ARG235
A	HOH418
A	LEU30
A	ASP32
A	GLY34
A	SER35
A	TYR71
A	THR72
A	GLN73
A	GLY74

---

site_id	AC2
Number of Residues	21
Details	BINDING SITE FOR RESIDUE PB0 B 394

Chain	Residue
B	GLY11
B	GLN12
B	GLY13
B	LEU30
B	ASP32
B	GLY34
B	SER35
B	TYR71
B	THR72
B	GLN73
B	GLY74
B	PHE108
B	ILE110
B	TRP115
B	TYR198
B	ASP228
B	GLY230
B	THR231
B	THR232
B	ARG235
B	HOH437

---

site_id	AC3
Number of Residues	18
Details	BINDING SITE FOR RESIDUE PB0 D 394

Chain	Residue
D	GLY11
D	GLN12
D	GLY13
D	ASP32
D	GLY34
D	TYR71
D	THR72
D	GLN73
D	GLY74
D	PHE108
D	ILE110
D	TRP115
D	TYR198
D	ASP228
D	GLY230
D	THR231
D	THR232
D	ARG235

---

site_id	AC4
Number of Residues	21
Details	BINDING SITE FOR RESIDUE PB0 E 394

Chain	Residue
E	GLY11
E	GLN12
E	GLY13
E	LEU30
E	ASP32
E	GLY34
E	SER35
E	TYR71
E	THR72
E	GLN73
E	GLY74
E	PHE108
E	ILE110
E	TRP115
E	TYR198
E	ASP228
E	GLY230
E	THR231
E	THR232
E	ARG235
E	HOH402

---

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	ILE29-VAL40

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094

Chain	Residue	Details
A	ASP32
A	ASP228
B	ASP32
B	ASP228
D	ASP32
D	ASP228
E	ASP32
E	ASP228

---

site_id	SWS_FT_FI2
Number of Residues	28
Details	MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241

Chain	Residue	Details
A	LYS65
B	LYS218
B	LYS224
B	LYS238
B	LYS239
B	LYS246
D	LYS65
D	LYS214
D	LYS218
D	LYS224
D	LYS238
A	LYS214
D	LYS239
D	LYS246
E	LYS65
E	LYS214
E	LYS218
E	LYS224
E	LYS238
E	LYS239
E	LYS246
A	LYS218
A	LYS224
A	LYS238
A	LYS239
A	LYS246
B	LYS65
B	LYS214

---

site_id	SWS_FT_FI3
Number of Residues	16
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN92
D	ASN111
D	ASN162
D	ASN293
E	ASN92
E	ASN111
E	ASN162
E	ASN293
A	ASN111
A	ASN162
A	ASN293
B	ASN92
B	ASN111
B	ASN162
B	ASN293
D	ASN92

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