4HZH
Structure of recombinant Gla-domainless prothrombin mutant S525A
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004252 | molecular_function | serine-type endopeptidase activity |
A | 0005509 | molecular_function | calcium ion binding |
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 | 0005576 | cellular_component | extracellular region |
B | 0006508 | biological_process | proteolysis |
B | 0007596 | biological_process | blood coagulation |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | ACT_SITE: Charge relay system |
Chain | Residue | Details |
A | HIS363 | |
A | ASP419 | |
A | ALA525 | |
B | HIS363 | |
B | ASP419 | |
B | ALA525 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | SITE: Cleavage; by thrombin |
Chain | Residue | Details |
A | ARG155 | |
B | ARG155 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | SITE: Cleavage; by factor Xa => ECO:0000269|PubMed:34265300 |
Chain | Residue | Details |
A | ARG271 | |
A | ARG320 | |
B | ARG271 | |
B | ARG320 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:22171320 |
Chain | Residue | Details |
A | ASN78 | |
A | ASN100 | |
B | ASN78 | |
B | ASN100 |
site_id | SWS_FT_FI5 |
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 |
A | ASN373 | |
B | ASN373 |