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 | 0008201 | molecular_function | heparin binding |
A | 0008236 | molecular_function | serine-type peptidase activity |
A | 0016020 | cellular_component | membrane |
A | 0030193 | biological_process | regulation of blood coagulation |
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 | 3 |
Details | ACT_SITE: Charge relay system |
Chain | Residue | Details |
A | HIS413 | |
A | ASP462 | |
A | SER557 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: |
Chain | Residue | Details |
A | LYS529 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:25092234 |
Chain | Residue | Details |
A | ASN72 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:25092234 |
Chain | Residue | Details |
A | ASN108 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine; atypical => ECO:0000269|PubMed:25092234 |
Chain | Residue | Details |
A | ASN145 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:25092234 |
Chain | Residue | Details |
A | ASN432 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:1998667, ECO:0000269|PubMed:25092234 |
Chain | Residue | Details |
A | ASN473 |