5EOD
Human Plasma Coagulation FXI with peptide LP2
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004252 | molecular_function | serine-type endopeptidase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006508 | biological_process | proteolysis |
| A | 0007596 | biological_process | blood coagulation |
| A | 0007599 | biological_process | hemostasis |
| A | 0008201 | molecular_function | heparin binding |
| A | 0008233 | molecular_function | peptidase activity |
| A | 0008236 | molecular_function | serine-type peptidase activity |
| A | 0016020 | cellular_component | membrane |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0031639 | biological_process | plasminogen activation |
| A | 0051919 | biological_process | positive regulation of fibrinolysis |
| A | 0070009 | molecular_function | serine-type aminopeptidase activity |
| A | 0070062 | cellular_component | extracellular exosome |
Functional Information from PROSITE/UniProt
| site_id | PS00134 |
| Number of Residues | 6 |
| Details | TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC |
| Chain | Residue | Details |
| A | LEU409-CYS414 |
| site_id | PS00135 |
| Number of Residues | 12 |
| Details | TRYPSIN_SER Serine proteases, trypsin family, serine active site. DAckGDSGGPLS |
| Chain | Residue | Details |
| A | ASP551-SER562 |
| site_id | PS00495 |
| Number of Residues | 84 |
| Details | APPLE Apple domain. CvtqLlkdtcFeggDIttvftpsakyCqvvCTyhprClLFtFtaespsedptrwftCvLKdSvtetlprvnrtaai.SGySFkqC |
| Chain | Residue | Details |
| A | CYS2-CYS85 | |
| A | CYS92-CYS175 | |
| A | CYS182-CYS265 | |
| A | CYS273-CYS356 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 83 |
| Details | Domain: {"description":"Apple 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00315","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 83 |
| Details | Domain: {"description":"Apple 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00315","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 83 |
| Details | Domain: {"description":"Apple 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00315","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Charge relay system"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"25092234","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25092234","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine; atypical","evidences":[{"source":"PubMed","id":"25092234","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25092234","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1998667","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25092234","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
