1ATH
THE INTACT AND CLEAVED HUMAN ANTITHROMBIN III COMPLEX AS A MODEL FOR SERPIN-PROTEINASE INTERACTIONS
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0002020 | molecular_function | protease binding |
| A | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005788 | cellular_component | endoplasmic reticulum lumen |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0007596 | biological_process | blood coagulation |
| A | 0008201 | molecular_function | heparin binding |
| A | 0030193 | biological_process | regulation of blood coagulation |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0062023 | cellular_component | collagen-containing extracellular matrix |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0072562 | cellular_component | blood microparticle |
| B | 0002020 | molecular_function | protease binding |
| B | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005615 | cellular_component | extracellular space |
| B | 0005788 | cellular_component | endoplasmic reticulum lumen |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0007596 | biological_process | blood coagulation |
| B | 0008201 | molecular_function | heparin binding |
| B | 0030193 | biological_process | regulation of blood coagulation |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0062023 | cellular_component | collagen-containing extracellular matrix |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 0072562 | cellular_component | blood microparticle |
Functional Information from PDB Data
| site_id | P1 |
| Number of Residues | 2 |
| Details | CLEAVAGE SITE BY SERINE PROTEASES LIKE THROMBIN |
| Chain | Residue |
| A | ARG393 |
| B | ARG393 |
Functional Information from PROSITE/UniProt
| site_id | PS00284 |
| Number of Residues | 11 |
| Details | SERPIN Serpins signature. FKANRPFLVfI |
| Chain | Residue | Details |
| A | PHE402-ILE412 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | TRP49 | |
| A | ARG129 | |
| A | ARG145 | |
| B | TRP49 | |
| B | ARG129 | |
| B | ARG145 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | SITE: Reactive bond => ECO:0000269|PubMed:7238875 |
| Chain | Residue | Details |
| A | ARG393 | |
| B | ARG393 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine; by FAM20C => ECO:0000269|PubMed:26091039 |
| Chain | Residue | Details |
| A | THR31 | |
| B | THR31 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039, ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SER36 | |
| B | SER36 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| 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 |
| A | ASN96 | |
| B | ASN96 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|Ref.10 |
| Chain | Residue | Details |
| A | ASN135 | |
| B | ASN135 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| 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 |
| A | ASN155 | |
| B | ASN155 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|Ref.10 |
| Chain | Residue | Details |
| A | ASN192 | |
| B | ASN192 |
