3LMS
Structure of human activated thrombin-activatable fibrinolysis inhibitor, TAFIa, in complex with tick-derived funnelin inhibitor, TCI.
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004181 | molecular_function | metallocarboxypeptidase activity |
A | 0006508 | biological_process | proteolysis |
A | 0008270 | molecular_function | zinc ion binding |
A | 0042730 | biological_process | fibrinolysis |
B | 0004857 | molecular_function | enzyme inhibitor activity |
B | 0005576 | cellular_component | extracellular region |
B | 0007596 | biological_process | blood coagulation |
B | 0008191 | molecular_function | metalloendopeptidase inhibitor activity |
B | 0010951 | biological_process | negative regulation of endopeptidase activity |
B | 0030414 | molecular_function | peptidase inhibitor activity |
B | 0035821 | biological_process | modulation of process of another organism |
B | 0044002 | biological_process | acquisition of nutrients from host |
B | 0090729 | molecular_function | toxin activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 309 |
Chain | Residue |
A | HIS69 |
A | GLU72 |
A | HIS196 |
B | LEU74 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GLY A 501 |
Chain | Residue |
B | LEU74 |
A | HIS69 |
A | ARG127 |
A | ASN144 |
A | ARG145 |
A | TYR248 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL B 502 |
Chain | Residue |
B | GLY39 |
B | CYS40 |
B | LYS41 |
B | SER63 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 503 |
Chain | Residue |
A | PHE132 |
A | ILE139 |
A | CYS166 |
A | GLY167 |
A | HOH526 |
A | HOH528 |
A | HOH530 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 504 |
Chain | Residue |
A | SER5 |
A | GLY84 |
A | HIS85 |
A | GLN88 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 505 |
Chain | Residue |
A | TRP73 |
A | ARG124 |
A | PHE279 |
A | LEU280 |
A | LEU281 |
B | GLY7 |
B | PHE8 |
site_id | AC7 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL A 506 |
Chain | Residue |
A | TYR118 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 507 |
Chain | Residue |
A | HIS137 |
A | SER160 |
A | CA509 |
site_id | AC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL B 508 |
Chain | Residue |
A | CA509 |
B | SER28 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA A 509 |
Chain | Residue |
A | LYS122 |
A | SER159 |
A | CYS161 |
A | CL507 |
B | CL508 |
site_id | BC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE K A 510 |
Chain | Residue |
A | GLN95 |
A | ARG306 |
site_id | BC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE K A 511 |
Chain | Residue |
A | ASN16 |
B | GLY67 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 297 |
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 | 1 |
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 | 7 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P00730","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
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 | 1 |
Details | Site: {"description":"Cleavage; by thrombin"} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; partial","evidences":[{"source":"PubMed","id":"16445295","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |