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8UF7

Cryo-EM structure of POmAb, a Type-I anti-prothrombin antiphospholipid antibody, bound to kringle-1 of human prothrombin

Functional Information from GO Data
ChainGOidnamespacecontents
C0001530molecular_functionlipopolysaccharide binding
C0004175molecular_functionendopeptidase activity
C0004252molecular_functionserine-type endopeptidase activity
C0005102molecular_functionsignaling receptor binding
C0005509molecular_functioncalcium ion binding
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005615cellular_componentextracellular space
C0005788cellular_componentendoplasmic reticulum lumen
C0005796cellular_componentGolgi lumen
C0005886cellular_componentplasma membrane
C0006508biological_processproteolysis
C0006953biological_processacute-phase response
C0007166biological_processcell surface receptor signaling pathway
C0007186biological_processG protein-coupled receptor signaling pathway
C0007596biological_processblood coagulation
C0007599biological_processhemostasis
C0008083molecular_functiongrowth factor activity
C0008201molecular_functionheparin binding
C0008233molecular_functionpeptidase activity
C0008236molecular_functionserine-type peptidase activity
C0009611biological_processresponse to wounding
C0009897cellular_componentexternal side of plasma membrane
C0010544biological_processnegative regulation of platelet activation
C0016787molecular_functionhydrolase activity
C0030168biological_processplatelet activation
C0030193biological_processregulation of blood coagulation
C0030194biological_processpositive regulation of blood coagulation
C0030195biological_processnegative regulation of blood coagulation
C0031012cellular_componentextracellular matrix
C0032967biological_processpositive regulation of collagen biosynthetic process
C0042730biological_processfibrinolysis
C0045861biological_processnegative regulation of proteolysis
C0046427biological_processpositive regulation of receptor signaling pathway via JAK-STAT
C0048018molecular_functionreceptor ligand activity
C0048712biological_processnegative regulation of astrocyte differentiation
C0050878biological_processregulation of body fluid levels
C0051281biological_processpositive regulation of release of sequestered calcium ion into cytosol
C0051480biological_processregulation of cytosolic calcium ion concentration
C0051918biological_processnegative regulation of fibrinolysis
C0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
C0070053molecular_functionthrombospondin receptor activity
C0070062cellular_componentextracellular exosome
C0070493biological_processthrombin-activated receptor signaling pathway
C0070945biological_processneutrophil-mediated killing of gram-negative bacterium
C0072562cellular_componentblood microparticle
C1900016biological_processnegative regulation of cytokine production involved in inflammatory response
C1900182biological_processpositive regulation of protein localization to nucleus
C1900738biological_processpositive regulation of phospholipase C-activating G protein-coupled receptor signaling pathway
C2000379biological_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
CGLU16-TRP41

site_idPS00021
Number of Residues14
DetailsKRINGLE_1 Kringle domain signature. FCRNpdssttgpWC
ChainResidueDetails
CPHE113-CYS126
CPHE218-CYS231

site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
CLEU359-CYS364

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DAceGDSGGPFV
ChainResidueDetails
CASP519-VAL530

site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCEATH
ChainResidueDetails
ATYR193-HIS199

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 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

249697

PDB entries from 2026-02-25

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