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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9P0X

Nanodisc-embedded human TF/FVIIa/XK1 in complex with 10H10 Fab (nanodisc-subtracted)

Functional Information from GO Data
ChainGOidnamespacecontents
T0001938biological_processpositive regulation of endothelial cell proliferation
T0002020molecular_functionprotease binding
T0002541biological_processactivation of plasma proteins involved in acute inflammatory response
T0002543biological_processactivation of blood coagulation via clotting cascade
T0004252molecular_functionserine-type endopeptidase activity
T0004896molecular_functioncytokine receptor activity
T0005515molecular_functionprotein binding
T0005543molecular_functionphospholipid binding
T0005576cellular_componentextracellular region
T0005615cellular_componentextracellular space
T0005886cellular_componentplasma membrane
T0006950biological_processresponse to stress
T0006974biological_processDNA damage response
T0007596biological_processblood coagulation
T0007599biological_processhemostasis
T0008643biological_processcarbohydrate transport
T0009897cellular_componentexternal side of plasma membrane
T0009986cellular_componentcell surface
T0010628biological_processpositive regulation of gene expression
T0010641biological_processpositive regulation of platelet-derived growth factor receptor signaling pathway
T0015768biological_processmaltose transport
T0016020cellular_componentmembrane
T0016485biological_processprotein processing
T0019221biological_processcytokine-mediated signaling pathway
T0030288cellular_componentouter membrane-bounded periplasmic space
T0030335biological_processpositive regulation of cell migration
T0031012cellular_componentextracellular matrix
T0032008biological_processpositive regulation of TOR signaling
T0032757biological_processpositive regulation of interleukin-8 production
T0034219biological_processcarbohydrate transmembrane transport
T0034289biological_processdetection of maltose stimulus
T0042597cellular_componentperiplasmic space
T0042956biological_processmaltodextrin transmembrane transport
T0043190cellular_componentATP-binding cassette (ABC) transporter complex
T0045766biological_processpositive regulation of angiogenesis
T0050927biological_processpositive regulation of positive chemotaxis
T0055052cellular_componentATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing
T0060326biological_processcell chemotaxis
T1901982molecular_functionmaltose binding
T1905286cellular_componentserine-type peptidase complex
T2000353biological_processpositive regulation of endothelial cell apoptotic process
Functional Information from PROSITE/UniProt
site_idPS00010
Number of Residues12
DetailsASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CkDglgeYtCtC
ChainResidueDetails
XCYS61-CYS72
VCYS61-CYS72
site_idPS00011
Number of Residues26
DetailsGLA_1 Vitamin K-dependent carboxylation domain. EcmEEtCsyeearEvfedsdktne.FW
ChainResidueDetails
XCGU16-TRP41
VCGU16-TRP41
site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CtCleGfeGKnC
ChainResidueDetails
XCYS70-CYS81
VCYS70-CYS81
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VSAAHC
ChainResidueDetails
SVAL189-CYS194
site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DSckGDSGGPHA
ChainResidueDetails
SASP338-ALA349
site_idPS00280
Number of Residues19
DetailsBPTI_KUNITZ_1 Pancreatic trypsin inhibitor (Kunitz) family signature. FiyGGCegnqnrFesleeC
ChainResidueDetails
KPHE54-CYS72
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCEATH
ChainResidueDetails
LTYR198-HIS204
site_idPS00621
Number of Residues18
DetailsTISSUE_FACTOR Tissue factor signature. WKsKCfyTtDTECDLTDE
ChainResidueDetails
TTRP45-GLU62
site_idPS01037
Number of Residues18
DetailsSBP_BACTERIAL_1 Bacterial extracellular solute-binding proteins, family 1 signature. PIAvEalSLIYNkdlLpN
ChainResidueDetails
TPRO357-ASN374
site_idPS01186
Number of Residues12
DetailsEGF_2 EGF-like domain signature 2. CtCleGFegkn....C
ChainResidueDetails
XCYS70-CYS81
XCYS109-CYS124
VCYS112-CYS127
site_idPS01187
Number of Residues25
DetailsEGF_CA Calcium-binding EGF-like domain signature. DgDQCetsp..........Cqnqgk..CkDglgeYtC
ChainResidueDetails
XASP46-CYS70
VASP46-CYS70
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues72
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 Residues1
DetailsModified residue: {"description":"4-carboxyglutamate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00463","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"6871167","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"(3R)-3-hydroxyaspartate","evidences":[{"source":"PubMed","id":"6871167","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues239
DetailsDomain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues3
DetailsActive site: {"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
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_FI13
Number of Residues6
DetailsMotif: {"description":"WKS motif"}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues50
DetailsDomain: {"description":"BPTI/Kunitz inhibitor 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00031","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues1
DetailsSite: {"description":"Reactive bond"}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues1
DetailsGlycosylation: {"description":"O-linked (GalNAc...) threonine; partial","evidences":[{"source":"PubMed","id":"19017259","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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PDB entries from 2026-01-14

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