4DV9

Crystal structure of BACE1 with its inhibitor

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	3
Details	BINDING SITE FOR RESIDUE SO4 A 401

Chain	Residue
A	ARG50
A	TYR51
A	GLN53

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site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 402

Chain	Residue
A	TYR51
A	GLN53
A	GLN55
A	LYS218
A	HOH725

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 403

Chain	Residue
A	GLU134
A	SER139
A	GLN143
A	HOH679
A	ARG96

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 404

Chain	Residue
A	SER22
A	PRO23
A	SER58
A	HIS145
A	PRO147
A	HOH554

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site_id	AC5
Number of Residues	26
Details	BINDING SITE FOR CHAIN B OF 8-MER PEPTIDE INHIBITOR

Chain	Residue
A	GLY11
A	LEU30
A	ASP32
A	GLY34
A	VAL69
A	PRO70
A	TYR71
A	THR72
A	GLN73
A	PHE108
A	ILE110
A	ILE126
A	LEU188
A	TYR190
A	TRP197
A	TYR198
A	ASP228
A	GLY230
A	THR231
A	THR232
A	ARG235
A	HOH547
A	HOH581
A	HOH593
A	HOH680
B	HOH101

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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	ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094

Chain	Residue	Details
A	ASP32
A	ASP228

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site_id	SWS_FT_FI2
Number of Residues	7
Details	MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241

Chain	Residue	Details
A	LYS65
A	LYS214
A	LYS218
A	LYS224
A	LYS238
A	LYS239
A	LYS246

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN92
A	ASN111
A	ASN162
A	ASN293

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