1JMJ
Crystal Structure of Native Heparin Cofactor II
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004866 | molecular_function | endopeptidase inhibitor activity |
A | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
A | 0005576 | cellular_component | extracellular region |
A | 0005615 | cellular_component | extracellular space |
A | 0005788 | cellular_component | endoplasmic reticulum lumen |
A | 0006935 | biological_process | chemotaxis |
A | 0007596 | biological_process | blood coagulation |
A | 0007599 | biological_process | hemostasis |
A | 0008201 | molecular_function | heparin binding |
A | 0030414 | molecular_function | peptidase inhibitor activity |
A | 0070062 | cellular_component | extracellular exosome |
B | 0004866 | molecular_function | endopeptidase inhibitor activity |
B | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
B | 0005576 | cellular_component | extracellular region |
B | 0005615 | cellular_component | extracellular space |
B | 0005788 | cellular_component | endoplasmic reticulum lumen |
B | 0006935 | biological_process | chemotaxis |
B | 0007596 | biological_process | blood coagulation |
B | 0007599 | biological_process | hemostasis |
B | 0008201 | molecular_function | heparin binding |
B | 0030414 | molecular_function | peptidase inhibitor activity |
B | 0070062 | cellular_component | extracellular exosome |
Functional Information from PROSITE/UniProt
site_id | PS00430 |
Number of Residues | 85 |
Details | TONB_DEPENDENT_REC_1 TonB-dependent receptor (TBDR) proteins signature 1. gskgpldqlekggetaqsadpqweqlnnknlsmpllpadfhkentvtndwipegeedddyldlekifsedddyidiv......................................DSLSVSPT |
Chain | Residue | Details |
A | GLY1-THR85 |
site_id | PS00284 |
Number of Residues | 11 |
Details | SERPIN Serpins signature. FTVDRPFLFlI |
Chain | Residue | Details |
A | PHE450-ILE460 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | SITE: Reactive bond => ECO:0000250 |
Chain | Residue | Details |
A | LEU444 | |
B | LEU444 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039 |
Chain | Residue | Details |
A | SER18 | |
B | SER18 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | MOD_RES: Sulfotyrosine => ECO:0000269|PubMed:12169660 |
Chain | Residue | Details |
A | TYR60 | |
A | TYR73 | |
B | TYR60 | |
B | TYR73 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218 |
Chain | Residue | Details |
A | ASN30 | |
B | ASN30 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12169660, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218 |
Chain | Residue | Details |
A | ASN169 | |
B | ASN169 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12169660 |
Chain | Residue | Details |
A | ASN368 | |
B | ASN368 |