3SKG

Crystal structure of beta-site app-cleaving enzyme 1 (BACE-WT) complex with (2S)-2-((3R)-3-acetamido-3-isobutyl-2-oxo-1-pyrrolidinyl)-N-((1S,2R)-1-(3,5-difluorobenzyl)-2-hydroxy-2-(1,2,3,4-tetrahydro-3-isoquinolinyl)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	17
Details	BINDING SITE FOR RESIDUE PB8 A 394

Chain	Residue
A	GLY11
A	ILE110
A	TRP115
A	TYR198
A	ASP228
A	GLY230
A	THR231
A	THR232
A	ARG235
A	GLN12
A	LEU30
A	ASP32
A	GLY34
A	TYR71
A	THR72
A	GLN73
A	PHE108

---

site_id	AC2
Number of Residues	18
Details	BINDING SITE FOR RESIDUE PB8 B 394

Chain	Residue
B	GLY11
B	GLY13
B	ASP32
B	GLY34
B	SER35
B	TYR71
B	THR72
B	GLN73
B	PHE108
B	ILE110
B	TRP115
B	TYR198
B	ASP228
B	GLY230
B	THR231
B	THR232
B	ARG235
B	HOH430

---

site_id	AC3
Number of Residues	18
Details	BINDING SITE FOR RESIDUE PB8 D 394

Chain	Residue
D	GLY11
D	LEU30
D	ASP32
D	GLY34
D	SER35
D	TYR71
D	THR72
D	GLN73
D	PHE108
D	ILE110
D	TRP115
D	TYR198
D	ILE226
D	ASP228
D	GLY230
D	THR231
D	THR232
D	ARG235

---

site_id	AC4
Number of Residues	19
Details	BINDING SITE FOR RESIDUE PB8 E 394

Chain	Residue
E	GLN12
E	GLY13
E	LEU30
E	ASP32
E	GLY34
E	TYR71
E	THR72
E	GLN73
E	LYS107
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

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1364
Details	Domain: {"description":"Peptidase A1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01103","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	28
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"17425515","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19011241","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	16
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---