3QDZ

Crystal structure of the human thrombin mutant D102N in complex with the extracellular fragment of human PAR4.

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
C	0004252	molecular_function	serine-type endopeptidase activity
C	0005576	cellular_component	extracellular region
C	0006508	biological_process	proteolysis
C	0007596	biological_process	blood coagulation
D	0004252	molecular_function	serine-type endopeptidase activity
D	0005509	molecular_function	calcium ion binding
D	0006508	biological_process	proteolysis
D	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

---

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

Chain	Residue	Details
B	ASP189-VAL200

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	SITE: Cleavage; by thrombin or trypsin => ECO:0000250

Chain	Residue	Details
E	ARG47
F	ARG47
B	SER195
D	HIS57
D	ASN102
D	SER195

---

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
D	ASN60

---