4Z6A
Crystal Structure of a FVIIa-Trypsin Chimera (YT) in Complex with Soluble Tissue Factor
Functional Information from GO Data
Functional Information from PROSITE/UniProt
site_id | PS00010 |
Number of Residues | 12 |
Details | ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CkDqlqsYiCfC |
Chain | Residue | Details |
L | CYS61-CYS72 |
site_id | PS00022 |
Number of Residues | 12 |
Details | EGF_1 EGF-like domain signature 1. CfClpAfeGRnC |
Chain | Residue | Details |
L | CYS70-CYS81 |
site_id | PS00134 |
Number of Residues | 6 |
Details | TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VSAAHC |
Chain | Residue | Details |
H | VAL53-CYS58 |
site_id | PS00135 |
Number of Residues | 12 |
Details | TRYPSIN_SER Serine proteases, trypsin family, serine active site. DSckGDSGGPHA |
Chain | Residue | Details |
H | ASP189-ALA200 |
site_id | PS00621 |
Number of Residues | 18 |
Details | TISSUE_FACTOR Tissue factor signature. WKsKCfyTtDTECDLTDE |
Chain | Residue | Details |
T | TRP45-GLU62 |
site_id | PS01186 |
Number of Residues | 16 |
Details | EGF_2 EGF-like domain signature 2. CrCheGYslladgvsC |
Chain | Residue | Details |
L | CYS112-CYS127 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | Site: {"description":"Important for S-112 for O-xylosylation"} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | Modified residue: {"description":"(3R)-3-hydroxyaspartate","evidences":[{"source":"PubMed","id":"3264725","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"O-linked (Xyl...) serine; alternate","evidences":[{"source":"PubMed","id":"1904059","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2129367","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21949356","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2511201","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"O-linked (Fuc) serine","featureId":"CAR_000180","evidences":[{"source":"PubMed","id":"1904059","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9023546","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 3 |
Details | Active site: {"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19167329","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3264725","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 6 |
Details | Motif: {"description":"WKS motif"} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |