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4NZQ

Crystal structure of Ca2+-free prothrombin deletion mutant residues 146-167

Functional Information from GO Data
ChainGOidnamespacecontents
A0001530molecular_functionlipopolysaccharide binding
A0001934biological_processpositive regulation of protein phosphorylation
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
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
A0030168biological_processplatelet activation
A0030193biological_processregulation of blood coagulation
A0030194biological_processpositive regulation of blood coagulation
A0030307biological_processpositive regulation of cell growth
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
A0048712biological_processnegative regulation of astrocyte differentiation
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
A0062023cellular_componentcollagen-containing extracellular matrix
A0070053molecular_functionthrombospondin receptor activity
A0070062cellular_componentextracellular exosome
A0070945biological_processneutrophil-mediated killing of gram-negative bacterium
A0072562cellular_componentblood microparticle
A0090218biological_processpositive regulation of lipid kinase activity
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_idPS00021
Number of Residues14
DetailsKRINGLE_1 Kringle domain signature. FCRNpdssttgpWC
ChainResidueDetails
APHE113-CYS126
APHE218-CYS231

site_idPS00011
Number of Residues26
DetailsGLA_1 Vitamin K-dependent carboxylation domain. EcvEEtCsyeeafEalesstatdv.FW
ChainResidueDetails
ACGU16-TRP41

site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
ALEU359-CYS364

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DAceGDSGGPFV
ChainResidueDetails
AASP519-VAL530

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Charge relay system
ChainResidueDetails
AHIS363
AASP419
ASER525

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Cleavage; by thrombin
ChainResidueDetails
AGLN177

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Cleavage; by factor Xa => ECO:0000269|PubMed:34265300
ChainResidueDetails
AARG271
AARG320

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: 4-carboxyglutamate => ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:3759958, ECO:0000269|PubMed:6305407
ChainResidueDetails
ACGU6
ACGU7

site_idSWS_FT_FI5
Number of Residues8
DetailsMOD_RES: 4-carboxyglutamate => ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:6305407
ChainResidueDetails
ACGU20
ACGU25
ACGU26
ACGU29
ACGU32
ACGU14
ACGU16
ACGU19

site_idSWS_FT_FI6
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:22171320
ChainResidueDetails
AASN78
AASN100

site_idSWS_FT_FI7
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:873923
ChainResidueDetails
AASN373

221051

PDB entries from 2024-06-12

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