3UDK

Crystal Structure of BACE with Compound 6

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	8
Details	BINDING SITE FOR RESIDUE 095 A 501

Chain	Residue
A	LEU30
A	ASP32
A	GLY34
A	GLN73
A	ILE226
A	ASP228
A	GLY230
A	VAL332

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site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO A 502

Chain	Residue
A	GLN143
A	GLU134

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site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO A 503

Chain	Residue
A	GLU219
A	TYR222

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site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PEG A 504

Chain	Residue
A	GLY11
A	GLN12
A	GLY13
A	TYR14
A	GLY230
A	THR232

---

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ZN A 505

Chain	Residue
A	ASP131
A	HIS397

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site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 506

Chain	Residue
A	GLU255
A	ASP390
A	HIS396
A	HIS398

---

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

Chain

Residue

Details

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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

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site_id	SWS_FT_FI3
Number of Residues	3
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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