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 | 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 | 0007599 | biological_process | hemostasis |
| A | 0008233 | molecular_function | peptidase activity |
| A | 0008237 | molecular_function | metallopeptidase activity |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0042730 | biological_process | fibrinolysis |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070062 | cellular_component | extracellular exosome |
| 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 | 0007599 | biological_process | hemostasis |
| B | 0008233 | molecular_function | peptidase activity |
| B | 0008237 | molecular_function | metallopeptidase activity |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0042730 | biological_process | fibrinolysis |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0070062 | cellular_component | extracellular exosome |
| 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 | 0007599 | biological_process | hemostasis |
| C | 0008233 | molecular_function | peptidase activity |
| C | 0008237 | molecular_function | metallopeptidase activity |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0042730 | biological_process | fibrinolysis |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0070062 | cellular_component | extracellular exosome |
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 |
