Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4Z6A

Crystal Structure of a FVIIa-Trypsin Chimera (YT) in Complex with Soluble Tissue Factor

Functional Information from GO Data
ChainGOidnamespacecontents
H0004252molecular_functionserine-type endopeptidase activity
H0006508biological_processproteolysis
L0005509molecular_functioncalcium ion binding
T0007596biological_processblood coagulation
T0016020cellular_componentmembrane
Functional Information from PROSITE/UniProt
site_idPS00010
Number of Residues12
DetailsASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CkDqlqsYiCfC
ChainResidueDetails
LCYS61-CYS72

site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CfClpAfeGRnC
ChainResidueDetails
LCYS70-CYS81

site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VSAAHC
ChainResidueDetails
HVAL53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DSckGDSGGPHA
ChainResidueDetails
HASP189-ALA200

site_idPS00621
Number of Residues18
DetailsTISSUE_FACTOR Tissue factor signature. WKsKCfyTtDTECDLTDE
ChainResidueDetails
TTRP45-GLU62

site_idPS01186
Number of Residues16
DetailsEGF_2 EGF-like domain signature 2. CrCheGYslladgvsC
ChainResidueDetails
LCYS112-CYS127

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsSite: {"description":"Important for S-112 for O-xylosylation"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsModified residue: {"description":"(3R)-3-hydroxyaspartate","evidences":[{"source":"PubMed","id":"3264725","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsGlycosylation: {"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"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsGlycosylation: {"description":"O-linked (Fuc) serine","featureId":"CAR_000180","evidences":[{"source":"PubMed","id":"1904059","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9023546","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues3
DetailsActive site: {"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19167329","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3264725","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues6
DetailsMotif: {"description":"WKS motif"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

PDB statisticsPDBj update infoContact PDBjnumon