5I3V

Crystal structure of BACE1 in complex with aminoquinoline compound 1

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	1
Details	binding site for residue IOD A 401

Chain	Residue
A	SER105

---

site_id	AC2
Number of Residues	1
Details	binding site for residue IOD A 402

Chain	Residue
A	LYS107

---

site_id	AC3
Number of Residues	2
Details	binding site for residue IOD A 403

Chain	Residue
A	HOH836
A	HOH836

---

site_id	AC4
Number of Residues	15
Details	binding site for residue 68M A 404

Chain	Residue
A	TRP76
A	LYS107
A	ILE118
A	ARG128
A	TYR198
A	ASP228
A	THR231
A	HOH636
A	HOH648
A	HOH703
A	ASP32
A	GLY34
A	VAL69
A	TYR71
A	LYS75

---

site_id	AC5
Number of Residues	8
Details	binding site for residue GOL A 405

Chain	Residue
A	ARG50
A	TYR51
A	GLN53
A	SER187
A	HOH506
A	HOH523
A	HOH629
A	HOH769

---

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	2
Details	Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	7
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_FI3
Number of Residues	3
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---