1P8J

CRYSTAL STRUCTURE OF THE PROPROTEIN CONVERTASE FURIN

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004252	molecular_function	serine-type endopeptidase activity
A	0006508	biological_process	proteolysis
A	0008236	molecular_function	serine-type peptidase activity
B	0004252	molecular_function	serine-type endopeptidase activity
B	0006508	biological_process	proteolysis
B	0008236	molecular_function	serine-type peptidase activity
C	0004252	molecular_function	serine-type endopeptidase activity
C	0006508	biological_process	proteolysis
C	0008236	molecular_function	serine-type peptidase activity
D	0004252	molecular_function	serine-type endopeptidase activity
D	0006508	biological_process	proteolysis
D	0008236	molecular_function	serine-type peptidase activity
E	0004252	molecular_function	serine-type endopeptidase activity
E	0006508	biological_process	proteolysis
E	0008236	molecular_function	serine-type peptidase activity
F	0004252	molecular_function	serine-type endopeptidase activity
F	0006508	biological_process	proteolysis
F	0008236	molecular_function	serine-type peptidase activity
G	0004252	molecular_function	serine-type endopeptidase activity
G	0006508	biological_process	proteolysis
G	0008236	molecular_function	serine-type peptidase activity
H	0004252	molecular_function	serine-type endopeptidase activity
H	0006508	biological_process	proteolysis
H	0008236	molecular_function	serine-type peptidase activity

Functional Information from PROSITE/UniProt

site_id	PS00136
Number of Residues	12
Details	SUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. VSILDDGIeknH

Chain	Residue	Details
A	VAL149-HIS160

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site_id	PS00137
Number of Residues	11
Details	SUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGTrCAGeVAA

Chain	Residue	Details
A	HIS194-ALA204

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site_id	PS00138
Number of Residues	11
Details	SUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSaSaPlAAG

Chain	Residue	Details
A	GLY366-GLY376

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	ACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240

Chain	Residue	Details
A	ASP153
D	ASP153
D	HIS194
D	SER368
E	ASP153
E	HIS194
E	SER368
F	ASP153
F	HIS194
F	SER368
G	ASP153
A	HIS194
G	HIS194
G	SER368
H	ASP153
H	HIS194
H	SER368
A	SER368
B	ASP153
B	HIS194
B	SER368
C	ASP153
C	HIS194
C	SER368

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site_id	SWS_FT_FI2
Number of Residues	72
Details	BINDING: BINDING => ECO:0000269|PubMed:12794637, ECO:0007744|PDB:1P8J

Chain	Residue	Details
A	ASP115
B	ASP115
B	ASP162
B	VAL205
B	ASN208
B	VAL210
B	GLY212
B	ASP258
B	ASP301
B	GLU331
C	ASP115
A	ASP162
C	ASP162
C	VAL205
C	ASN208
C	VAL210
C	GLY212
C	ASP258
C	ASP301
C	GLU331
D	ASP115
D	ASP162
A	VAL205
D	VAL205
D	ASN208
D	VAL210
D	GLY212
D	ASP258
D	ASP301
D	GLU331
E	ASP115
E	ASP162
E	VAL205
A	ASN208
E	ASN208
E	VAL210
E	GLY212
E	ASP258
E	ASP301
E	GLU331
F	ASP115
F	ASP162
F	VAL205
F	ASN208
A	VAL210
F	VAL210
F	GLY212
F	ASP258
F	ASP301
F	GLU331
G	ASP115
G	ASP162
G	VAL205
G	ASN208
G	VAL210
A	GLY212
G	GLY212
G	ASP258
G	ASP301
G	GLU331
H	ASP115
H	ASP162
H	VAL205
H	ASN208
H	VAL210
H	GLY212
A	ASP258
H	ASP258
H	ASP301
H	GLU331
A	ASP301
A	GLU331

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site_id	SWS_FT_FI3
Number of Residues	72
Details	BINDING: BINDING => ECO:0000305|PubMed:12794637, ECO:0007744|PDB:1P8J

Chain	Residue	Details
A	ASP154
B	ASP154
B	ASP191
B	GLU236
B	SER253
B	ASP264
B	ALA292
B	ASP306
B	TYR308
B	SER368
C	ASP154
A	ASP191
C	ASP191
C	GLU236
C	SER253
C	ASP264
C	ALA292
C	ASP306
C	TYR308
C	SER368
D	ASP154
D	ASP191
A	GLU236
D	GLU236
D	SER253
D	ASP264
D	ALA292
D	ASP306
D	TYR308
D	SER368
E	ASP154
E	ASP191
E	GLU236
A	SER253
E	SER253
E	ASP264
E	ALA292
E	ASP306
E	TYR308
E	SER368
F	ASP154
F	ASP191
F	GLU236
F	SER253
A	ASP264
F	ASP264
F	ALA292
F	ASP306
F	TYR308
F	SER368
G	ASP154
G	ASP191
G	GLU236
G	SER253
G	ASP264
A	ALA292
G	ALA292
G	ASP306
G	TYR308
G	SER368
H	ASP154
H	ASP191
H	GLU236
H	SER253
H	ASP264
H	ALA292
A	ASP306
H	ASP306
H	TYR308
H	SER368
A	TYR308
A	SER368

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site_id	SWS_FT_FI4
Number of Residues	24
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P09958

Chain	Residue	Details
A	ASP174
D	ASP174
D	ASP179
D	ASP181
E	ASP174
E	ASP179
E	ASP181
F	ASP174
F	ASP179
F	ASP181
G	ASP174
A	ASP179
G	ASP179
G	ASP181
H	ASP174
H	ASP179
H	ASP181
A	ASP181
B	ASP174
B	ASP179
B	ASP181
C	ASP174
C	ASP179
C	ASP181

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site_id	SWS_FT_FI5
Number of Residues	16
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12794637, ECO:0007744|PDB:1P8J

Chain	Residue	Details
A	ASN387
E	ASN440
F	ASN387
F	ASN440
G	ASN387
G	ASN440
H	ASN387
H	ASN440
A	ASN440
B	ASN387
B	ASN440
C	ASN387
C	ASN440
D	ASN387
D	ASN440
E	ASN387

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