5V0N

BACE1 in complex with inhibitor 5g

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
C	0004190	molecular_function	aspartic-type endopeptidase activity
C	0006508	biological_process	proteolysis
C	0016020	cellular_component	membrane

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue SO4 A 401

Chain	Residue
A	ARG235
A	SER327
A	SER328
A	HOH502
A	HOH565

---

site_id	AC2
Number of Residues	6
Details	binding site for residue SO4 A 402

Chain	Residue
A	HOH555
A	HOH635
A	PHE47
A	LYS107
A	HOH503
A	HOH507

---

site_id	AC3
Number of Residues	3
Details	binding site for residue SO4 A 403

Chain	Residue
A	ARG96
A	GLU134
A	HOH511

---

site_id	AC4
Number of Residues	17
Details	binding site for residue 8W4 A 404

Chain	Residue
A	GLY11
A	LEU30
A	ASP32
A	GLY34
A	SER35
A	TYR71
A	THR72
A	GLN73
A	ILE126
A	TYR198
A	ASP228
A	GLY230
A	THR231
A	THR232
A	ASN233
A	ARG235
A	SER325

---

site_id	AC5
Number of Residues	3
Details	binding site for residue URE A 405

Chain	Residue
A	ARG307
A	LYS321
A	HOH522

---

site_id	AC6
Number of Residues	5
Details	binding site for residue SO4 B 401

Chain	Residue
B	ARG235
B	GLN326
B	SER327
B	SER328
B	HOH502

---

site_id	AC7
Number of Residues	6
Details	binding site for residue SO4 B 402

Chain	Residue
B	ARG96
B	ALA97
B	ASN98
B	GLU134
B	HOH528
B	HOH568

---

site_id	AC8
Number of Residues	4
Details	binding site for residue SO4 B 403

Chain	Residue
B	ARG50
B	TYR51
B	GLN53
B	HOH508

---

site_id	AC9
Number of Residues	4
Details	binding site for residue SO4 B 404

Chain	Residue
B	ASN293
B	LEU377
B	HOH526
C	ARG205

---

site_id	AD1
Number of Residues	7
Details	binding site for residue GOL B 405

Chain	Residue
B	ARG205
B	VAL375
B	THR376
B	HOH560
C	THR292
C	ASP378
C	HOH539

---

site_id	AD2
Number of Residues	15
Details	binding site for residue 8W4 B 406

Chain	Residue
B	ASP32
B	GLY34
B	SER35
B	TYR71
B	THR72
B	GLN73
B	ILE126
B	TYR198
B	ASP228
B	GLY230
B	THR231
B	THR232
B	ASN233
B	ARG235
B	SER325

---

site_id	AD3
Number of Residues	2
Details	binding site for residue URE B 407

Chain	Residue
B	GLU219
B	TYR222

---

site_id	AD4
Number of Residues	4
Details	binding site for residue SO4 C 401

Chain	Residue
C	VAL3
C	GLN153
C	HOH526
C	HOH540

---

site_id	AD5
Number of Residues	3
Details	binding site for residue SO4 C 402

Chain	Residue
B	GLU371
C	ASN293
C	GLN294

---

site_id	AD6
Number of Residues	5
Details	binding site for residue SO4 C 403

Chain	Residue
C	ARG96
C	ALA97
C	ASN98
C	GLU134
C	HOH514

---

site_id	AD7
Number of Residues	2
Details	binding site for residue SO4 C 404

Chain	Residue
C	ARG61
C	HOH536

---

site_id	AD8
Number of Residues	16
Details	binding site for residue 8W4 C 405

Chain	Residue
C	TYR198
C	ASP228
C	GLY230
C	THR231
C	THR232
C	ASN233
C	ARG235
C	SER325
C	GLY11
C	ASP32
C	GLY34
C	SER35
C	TYR71
C	THR72
C	GLN73
C	ILE126

---

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	6
Details	Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	21
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	9
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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