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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

1FAK

HUMAN TISSUE FACTOR COMPLEXED WITH COAGULATION FACTOR VIIA INHIBITED WITH A BPTI-MUTANT

Functional Information from GO Data
ChainGOidnamespacecontents
H0004252molecular_functionserine-type endopeptidase activity
H0006508biological_processproteolysis
I0004867molecular_functionserine-type endopeptidase inhibitor activity
L0005509molecular_functioncalcium ion binding
L0005576cellular_componentextracellular region
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_idPS00011
Number of Residues26
DetailsGLA_1 Vitamin K-dependent carboxylation domain. EckEEqCsfeearEifkdaertkl.FW
ChainResidueDetails
LCGU16-TRP41
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_idPS00280
Number of Residues19
DetailsBPTI_KUNITZ_1 Pancreatic trypsin inhibitor (Kunitz) family signature. FyyGGClakrnnFesaedC
ChainResidueDetails
IPHE33-CYS51
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
site_idPS01187
Number of Residues25
DetailsEGF_CA Calcium-binding EGF-like domain signature. DgDQCassp..........Cqnggs..CkDqlqsYiC
ChainResidueDetails
LASP46-CYS70
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues36
DetailsDomain: {"description":"EGF-like 1; calcium-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues1
DetailsSite: {"description":"Important for S-112 for O-xylosylation"}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"4-carboxyglutamate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00463","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"3264725","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3486420","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"(3R)-3-hydroxyaspartate","evidences":[{"source":"PubMed","id":"3264725","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
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_FI6
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_FI7
Number of Residues3
DetailsActive site: {"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
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_FI10
Number of Residues4
DetailsMotif: {"description":"WKS motif"}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues50
DetailsDomain: {"description":"BPTI/Kunitz inhibitor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00031","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues1
DetailsSite: {"description":"Reactive bond for trypsin"}
ChainResidueDetails
Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
HASP102
HHIS57
site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
HSER195
HGLY196
site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
HSER195
HGLY193
site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
HASP102
HSER195
HHIS57
site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
HASP102
HSER195
HHIS57
HGLY196
site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
HASP102
HSER195
HGLY193
HHIS57

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PDB entries from 2025-10-29

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