1TB6
2.5A Crystal Structure of the Antithrombin-Thrombin-Heparin Ternary Complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
H | 0004252 | molecular_function | serine-type endopeptidase activity |
H | 0005509 | molecular_function | calcium ion binding |
H | 0006508 | biological_process | proteolysis |
H | 0007596 | biological_process | blood coagulation |
I | 0002020 | molecular_function | protease binding |
I | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
I | 0005515 | molecular_function | protein binding |
I | 0005576 | cellular_component | extracellular region |
I | 0005615 | cellular_component | extracellular space |
I | 0005788 | cellular_component | endoplasmic reticulum lumen |
I | 0005886 | cellular_component | plasma membrane |
I | 0007596 | biological_process | blood coagulation |
I | 0007599 | biological_process | hemostasis |
I | 0008201 | molecular_function | heparin binding |
I | 0030193 | biological_process | regulation of blood coagulation |
I | 0030414 | molecular_function | peptidase inhibitor activity |
I | 0042802 | molecular_function | identical protein binding |
I | 0062023 | cellular_component | collagen-containing extracellular matrix |
I | 0070062 | cellular_component | extracellular exosome |
I | 0072562 | cellular_component | blood microparticle |
L | 0004252 | molecular_function | serine-type endopeptidase activity |
L | 0005576 | cellular_component | extracellular region |
L | 0006508 | biological_process | proteolysis |
L | 0007596 | biological_process | blood coagulation |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | ACT_SITE: Charge relay system |
Chain | Residue | Details |
H | HIS57 | |
H | ASP102 | |
H | ALA195 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
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 |
H | ASN60 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; by FAM20C => ECO:0000269|PubMed:26091039 |
Chain | Residue | Details |
I | THR31 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039, ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
I | SER36 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|Ref.10 |
Chain | Residue | Details |
I | ASN96 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|Ref.10 |
Chain | Residue | Details |
I | ASN135 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|Ref.10 |
Chain | Residue | Details |
I | ASN155 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|Ref.10 |
Chain | Residue | Details |
I | ASN192 |