9ZQY
Structural insights into the exosite-mediated activation of Factor IX by Factor XIa using cryoEM
Functional Information from PROSITE/UniProt
| site_id | PS00010 |
| Number of Residues | 12 |
| Details | ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CkDdinsYeCwC |
| Chain | Residue | Details |
| C | CYS62-CYS73 |
| site_id | PS00011 |
| Number of Residues | 26 |
| Details | GLA_1 Vitamin K-dependent carboxylation domain. EcmEEkCsfeearEvfentertte.FW |
| Chain | Residue | Details |
| C | CGU17-TRP42 |
| site_id | PS00022 |
| Number of Residues | 12 |
| Details | EGF_1 EGF-like domain signature 1. CwCpfGfeGKnC |
| Chain | Residue | Details |
| C | CYS71-CYS82 |
| site_id | PS00134 |
| Number of Residues | 6 |
| Details | TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC |
| Chain | Residue | Details |
| B | LEU409-CYS414 | |
| C | VAL217-CYS222 |
| site_id | PS00135 |
| Number of Residues | 12 |
| Details | TRYPSIN_SER Serine proteases, trypsin family, serine active site. DScqGDSGGPHV |
| Chain | Residue | Details |
| C | ASP359-VAL370 |
| 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 |
| site_id | PS01186 |
| Number of Residues | 12 |
| Details | EGF_2 EGF-like domain signature 2. CwCpfGFegkn....C |
| Chain | Residue | Details |
| C | CYS71-CYS82 | |
| C | CYS109-CYS124 |
| site_id | PS01187 |
| Number of Residues | 25 |
| Details | EGF_CA Calcium-binding EGF-like domain signature. DgDQCesnp..........Clnggs..CkDdinsYeC |
| Chain | Residue | Details |
| C | ASP47-CYS71 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 166 |
| 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 | 166 |
| 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 | 166 |
| 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 | 166 |
| Details | Domain: {"description":"Apple 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00315","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"25092234","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| 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_FI7 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine; atypical","evidences":[{"source":"PubMed","id":"25092234","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 470 |
| Details | Domain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 6 |
| Details | Active site: {"description":"Charge relay system"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 6 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| 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_FI12 |
| Number of Residues | 2 |
| 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 |
