5XG4

Crystal structure of uPA in complex with quercetin

Functional Information from GO Data

Chain	GOid	namespace	contents
U	0004252	molecular_function	serine-type endopeptidase activity
U	0006508	biological_process	proteolysis

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	binding site for residue QUE U 301

Chain	Residue
U	HIS57
U	GLY216
U	GLY219
U	PG6302
U	HIS99
U	ASP189
U	SER190
U	GLN192
U	SER195
U	VAL213
U	SER214
U	TRP215

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site_id	AC2
Number of Residues	7
Details	binding site for residue PG6 U 302

Chain	Residue
U	ARG35
U	HIS57
U	GLN192
U	GLY193
U	ASP194
U	SER195
U	QUE301

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Functional Information from PROSITE/UniProt

site_id	PS00134
Number of Residues	6
Details	TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. ISATHC

Chain	Residue	Details
U	ILE53-CYS58

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site_id	PS00135
Number of Residues	12
Details	TRYPSIN_SER Serine proteases, trypsin family, serine active site. DScqGDSGGPLV

Chain	Residue	Details
U	ASP189-VAL200

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	245
Details	Domain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	3
Details	Active site: {"description":"Charge relay system"}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"9151681","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","featureId":"CAR_000026"}

Chain

Residue

Details

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