3D68

Crystal structure of a T325I/T329I/H333Y/H335Q mutant of Thrombin-Activatable Fibrinolysis Inhibitor (TAFI-IIYQ)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003331	biological_process	positive regulation of extracellular matrix constituent secretion
A	0004180	molecular_function	carboxypeptidase activity
A	0004181	molecular_function	metallocarboxypeptidase activity
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0006508	biological_process	proteolysis
A	0007596	biological_process	blood coagulation
A	0008237	molecular_function	metallopeptidase activity
A	0008270	molecular_function	zinc ion binding
A	0009410	biological_process	response to xenobiotic stimulus
A	0010757	biological_process	negative regulation of plasminogen activation
A	0030163	biological_process	protein catabolic process
A	0042730	biological_process	fibrinolysis
A	0046872	molecular_function	metal ion binding
A	0051918	biological_process	negative regulation of fibrinolysis
A	0070062	cellular_component	extracellular exosome
A	0071333	biological_process	cellular response to glucose stimulus
A	0097421	biological_process	liver regeneration
A	2000346	biological_process	negative regulation of hepatocyte proliferation
B	0003331	biological_process	positive regulation of extracellular matrix constituent secretion
B	0004180	molecular_function	carboxypeptidase activity
B	0004181	molecular_function	metallocarboxypeptidase activity
B	0005576	cellular_component	extracellular region
B	0005615	cellular_component	extracellular space
B	0006508	biological_process	proteolysis
B	0007596	biological_process	blood coagulation
B	0008237	molecular_function	metallopeptidase activity
B	0008270	molecular_function	zinc ion binding
B	0009410	biological_process	response to xenobiotic stimulus
B	0010757	biological_process	negative regulation of plasminogen activation
B	0030163	biological_process	protein catabolic process
B	0042730	biological_process	fibrinolysis
B	0046872	molecular_function	metal ion binding
B	0051918	biological_process	negative regulation of fibrinolysis
B	0070062	cellular_component	extracellular exosome
B	0071333	biological_process	cellular response to glucose stimulus
B	0097421	biological_process	liver regeneration
B	2000346	biological_process	negative regulation of hepatocyte proliferation
C	0003331	biological_process	positive regulation of extracellular matrix constituent secretion
C	0004180	molecular_function	carboxypeptidase activity
C	0004181	molecular_function	metallocarboxypeptidase activity
C	0005576	cellular_component	extracellular region
C	0005615	cellular_component	extracellular space
C	0006508	biological_process	proteolysis
C	0007596	biological_process	blood coagulation
C	0008237	molecular_function	metallopeptidase activity
C	0008270	molecular_function	zinc ion binding
C	0009410	biological_process	response to xenobiotic stimulus
C	0010757	biological_process	negative regulation of plasminogen activation
C	0030163	biological_process	protein catabolic process
C	0042730	biological_process	fibrinolysis
C	0046872	molecular_function	metal ion binding
C	0051918	biological_process	negative regulation of fibrinolysis
C	0070062	cellular_component	extracellular exosome
C	0071333	biological_process	cellular response to glucose stimulus
C	0097421	biological_process	liver regeneration
C	2000346	biological_process	negative regulation of hepatocyte proliferation

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	ACT_SITE: Proton donor/acceptor => ECO:0000255|PROSITE-ProRule:PRU01379

Chain	Residue	Details
A	GLU363
B	GLU363
C	GLU363

---

site_id	SWS_FT_FI2
Number of Residues	9
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01379, ECO:0000269|PubMed:18559974, ECO:0000269|PubMed:20088943

Chain	Residue	Details
A	HIS159
A	GLU162
A	HIS288
B	HIS159
B	GLU162
B	HIS288
C	HIS159
C	GLU162
C	HIS288

---

site_id	SWS_FT_FI3
Number of Residues	12
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P00730

Chain	Residue	Details
A	ARG217
C	ASN234
C	SER289
C	TYR341
A	ASN234
A	SER289
A	TYR341
B	ARG217
B	ASN234
B	SER289
B	TYR341
C	ARG217

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	SITE: Cleavage; by thrombin

Chain	Residue	Details
A	ARG302
B	ARG302
C	ARG302

---

site_id	SWS_FT_FI5
Number of Residues	6
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16445295, ECO:0000269|PubMed:18559974

Chain	Residue	Details
A	ASN22
A	ASN51
B	ASN22
B	ASN51
C	ASN22
C	ASN51

---

site_id	SWS_FT_FI6
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16445295, ECO:0000269|PubMed:18559974

Chain	Residue	Details
A	ASN63
B	ASN63
C	ASN63

---

site_id	SWS_FT_FI7
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16445295, ECO:0000269|PubMed:18559974, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:22171320

Chain	Residue	Details
A	ASN86
B	ASN86
C	ASN86

---

site_id	SWS_FT_FI8
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine; partial => ECO:0000269|PubMed:16445295

Chain	Residue	Details
A	ASN219
B	ASN219
C	ASN219

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1cbx

Chain	Residue	Details
A	GLU363
A	ARG217

---

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1cbx

Chain	Residue	Details
B	GLU363
B	ARG217

---

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1cbx

Chain	Residue	Details
C	GLU363
C	ARG217

---

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1cbx

Chain	Residue	Details
A	ARG161
A	GLU363
A	ARG217

---

site_id	CSA5
Number of Residues	3
Details	Annotated By Reference To The Literature 1cbx

Chain	Residue	Details
B	ARG161
B	GLU363
B	ARG217

---

site_id	CSA6
Number of Residues	3
Details	Annotated By Reference To The Literature 1cbx

Chain	Residue	Details
C	ARG161
C	GLU363
C	ARG217

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