3RTM

Structure of Bace-1 (Beta-Secretase) in Complex with 3-(2-Aminoquinolin-3-yl)-N-cyclohexyl-N-methylpropanamide

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 1502

Chain	Residue
A	SER105

---

site_id	AC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE IOD A 1503

Chain	Residue
A	LYS107

---

site_id	AC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE IOD A 1505

Chain	Residue
A	ARG349

---

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL A 393

Chain	Residue
A	ARG50
A	TYR51
A	GLN53

---

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 394

Chain	Residue
A	VAL170
A	THR232
A	ARG307
A	GLU339
A	LYS9
A	GLY11
A	GLY13

---

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE RTM A 395

Chain	Residue
A	ASP32
A	SER35
A	ILE118
A	ASP228
A	GLY230
A	THR231

---

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

---