3BEF

Crystal structure of thrombin bound to the extracellular fragment of PAR1

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004252	molecular_function	serine-type endopeptidase activity
A	0005576	cellular_component	extracellular region
A	0006508	biological_process	proteolysis
A	0007596	biological_process	blood coagulation
B	0004252	molecular_function	serine-type endopeptidase activity
B	0005509	molecular_function	calcium ion binding
B	0006508	biological_process	proteolysis
B	0007596	biological_process	blood coagulation
D	0004252	molecular_function	serine-type endopeptidase activity
D	0005576	cellular_component	extracellular region
D	0006508	biological_process	proteolysis
D	0007596	biological_process	blood coagulation
E	0004252	molecular_function	serine-type endopeptidase activity
E	0005509	molecular_function	calcium ion binding
E	0006508	biological_process	proteolysis
E	0007596	biological_process	blood coagulation

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
B	LEU53-CYS58

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

Chain	Residue	Details
B	ASP189-VAL200

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	SITE: Cleavage; by CTSG => ECO:0000269|PubMed:7744748

Chain	Residue	Details
C	PHE55
F	PHE55
B	SER195
E	HIS57
E	ASN102
E	SER195

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site_id	SWS_FT_FI2
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:873923

Chain	Residue	Details
B	ASN60
E	ASN60

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