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 | 891 |
Details | Domain: {"description":"Peptidase M14","evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 21 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P00730","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 9 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18559974","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20088943","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 3 |
Details | Site: {"description":"Cleavage; by thrombin"} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 6 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16445295","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18559974","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 3 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16445295","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18559974","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 3 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16445295","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18559974","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22171320","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 3 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; partial","evidences":[{"source":"PubMed","id":"16445295","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
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 |