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5EDK

Crystal structure of prothrombin deletion mutant residues 146-167 ( Form II ).

Functional Information from GO Data
ChainGOidnamespacecontents
A0001530molecular_functionlipopolysaccharide binding
A0004175molecular_functionendopeptidase activity
A0004252molecular_functionserine-type endopeptidase activity
A0005102molecular_functionsignaling receptor binding
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005788cellular_componentendoplasmic reticulum lumen
A0005796cellular_componentGolgi lumen
A0005886cellular_componentplasma membrane
A0006508biological_processproteolysis
A0006953biological_processacute-phase response
A0007166biological_processcell surface receptor signaling pathway
A0007186biological_processG protein-coupled receptor signaling pathway
A0007596biological_processblood coagulation
A0007599biological_processhemostasis
A0008083molecular_functiongrowth factor activity
A0008201molecular_functionheparin binding
A0008233molecular_functionpeptidase activity
A0008236molecular_functionserine-type peptidase activity
A0008284biological_processpositive regulation of cell population proliferation
A0008360biological_processregulation of cell shape
A0009611biological_processresponse to wounding
A0009897cellular_componentexternal side of plasma membrane
A0010468biological_processregulation of gene expression
A0010544biological_processnegative regulation of platelet activation
A0016787molecular_functionhydrolase activity
A0030168biological_processplatelet activation
A0030193biological_processregulation of blood coagulation
A0030194biological_processpositive regulation of blood coagulation
A0030195biological_processnegative regulation of blood coagulation
A0030307biological_processpositive regulation of cell growth
A0031012cellular_componentextracellular matrix
A0032024biological_processpositive regulation of insulin secretion
A0032967biological_processpositive regulation of collagen biosynthetic process
A0042730biological_processfibrinolysis
A0045861biological_processnegative regulation of proteolysis
A0046427biological_processpositive regulation of receptor signaling pathway via JAK-STAT
A0048018molecular_functionreceptor ligand activity
A0048712biological_processnegative regulation of astrocyte differentiation
A0050878biological_processregulation of body fluid levels
A0051281biological_processpositive regulation of release of sequestered calcium ion into cytosol
A0051480biological_processregulation of cytosolic calcium ion concentration
A0051838biological_processcytolysis by host of symbiont cells
A0051897biological_processpositive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
A0051918biological_processnegative regulation of fibrinolysis
A0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
A0070053molecular_functionthrombospondin receptor activity
A0070062cellular_componentextracellular exosome
A0070493biological_processthrombin-activated receptor signaling pathway
A0070945biological_processneutrophil-mediated killing of gram-negative bacterium
A0072378biological_processblood coagulation, fibrin clot formation
A0072562cellular_componentblood microparticle
A1900016biological_processnegative regulation of cytokine production involved in inflammatory response
A1900182biological_processpositive regulation of protein localization to nucleus
A1900738biological_processpositive regulation of phospholipase C-activating G protein-coupled receptor signaling pathway
A1990806biological_processligand-gated ion channel signaling pathway
A2000379biological_processpositive regulation of reactive oxygen species metabolic process
Functional Information from PROSITE/UniProt
site_idPS00011
Number of Residues26
DetailsGLA_1 Vitamin K-dependent carboxylation domain. EcvEEtCsyeeafEalesstatdv.FW
ChainResidueDetails
ACGU16-TRP41

site_idPS00021
Number of Residues14
DetailsKRINGLE_1 Kringle domain signature. FCRNpdsstmgpWC
ChainResidueDetails
APHE113-CYS126
APHE196-CYS209

site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
ALEU337-CYS342

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DAceGDSGGPFV
ChainResidueDetails
AASP497-VAL508

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues78
DetailsDomain: {"description":"Kringle 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00121","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues22
DetailsRegion: {"description":"High affinity receptor-binding region which is also known as the TP508 peptide"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsActive site: {"description":"Charge relay system"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsSite: {"description":"Cleavage; by factor Xa","evidences":[{"source":"PubMed","id":"34265300","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"14760718","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22171320","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19838169","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"873923","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

242500

PDB entries from 2025-10-01

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