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7TPP

Cryo-em structure of human prothrombin:prothrombinase at 4.1 Angstrom resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
A0005576cellular_componentextracellular region
B0004252molecular_functionserine-type endopeptidase activity
B0006508biological_processproteolysis
C0005507molecular_functioncopper ion binding
D0005507molecular_functioncopper ion binding
E0001530molecular_functionlipopolysaccharide binding
E0001934biological_processpositive regulation of protein phosphorylation
E0004175molecular_functionendopeptidase activity
E0004252molecular_functionserine-type endopeptidase activity
E0005102molecular_functionsignaling receptor binding
E0005509molecular_functioncalcium ion binding
E0005515molecular_functionprotein binding
E0005576cellular_componentextracellular region
E0005615cellular_componentextracellular space
E0005788cellular_componentendoplasmic reticulum lumen
E0005796cellular_componentGolgi lumen
E0005886cellular_componentplasma membrane
E0006508biological_processproteolysis
E0006953biological_processacute-phase response
E0007166biological_processcell surface receptor signaling pathway
E0007186biological_processG protein-coupled receptor signaling pathway
E0007596biological_processblood coagulation
E0008083molecular_functiongrowth factor activity
E0008201molecular_functionheparin binding
E0008233molecular_functionpeptidase activity
E0008236molecular_functionserine-type peptidase activity
E0008284biological_processpositive regulation of cell population proliferation
E0008360biological_processregulation of cell shape
E0009611biological_processresponse to wounding
E0009897cellular_componentexternal side of plasma membrane
E0010468biological_processregulation of gene expression
E0010544biological_processnegative regulation of platelet activation
E0030168biological_processplatelet activation
E0030193biological_processregulation of blood coagulation
E0030194biological_processpositive regulation of blood coagulation
E0030307biological_processpositive regulation of cell growth
E0032024biological_processpositive regulation of insulin secretion
E0032967biological_processpositive regulation of collagen biosynthetic process
E0042730biological_processfibrinolysis
E0045861biological_processnegative regulation of proteolysis
E0046427biological_processpositive regulation of receptor signaling pathway via JAK-STAT
E0048712biological_processnegative regulation of astrocyte differentiation
E0051281biological_processpositive regulation of release of sequestered calcium ion into cytosol
E0051480biological_processregulation of cytosolic calcium ion concentration
E0051838biological_processcytolysis by host of symbiont cells
E0051897biological_processpositive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
E0051918biological_processnegative regulation of fibrinolysis
E0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
E0062023cellular_componentcollagen-containing extracellular matrix
E0070053molecular_functionthrombospondin receptor activity
E0070062cellular_componentextracellular exosome
E0070945biological_processneutrophil-mediated killing of gram-negative bacterium
E0072562cellular_componentblood microparticle
E0090218biological_processpositive regulation of lipid kinase activity
E1900016biological_processnegative regulation of cytokine production involved in inflammatory response
E1900182biological_processpositive regulation of protein localization to nucleus
E1900738biological_processpositive regulation of phospholipase C-activating G protein-coupled receptor signaling pathway
E1990806biological_processligand-gated ion channel signaling pathway
E2000379biological_processpositive regulation of reactive oxygen species metabolic process
Functional Information from PROSITE/UniProt
site_idPS00010
Number of Residues12
DetailsASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CkDglgeYtCtC
ChainResidueDetails
ACYS61-CYS72

site_idPS00011
Number of Residues26
DetailsGLA_1 Vitamin K-dependent carboxylation domain. EcmEEtCsyeearEvfedsdktne.FW
ChainResidueDetails
AGLU16-TRP41
EGLU16-TRP41

site_idPS00021
Number of Residues14
DetailsKRINGLE_1 Kringle domain signature. FCRNpdssttgpWC
ChainResidueDetails
EPHE113-CYS126
EPHE218-CYS231

site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CtCleGfeGKnC
ChainResidueDetails
ACYS70-CYS81

site_idPS00079
Number of Residues21
DetailsMULTICOPPER_OXIDASE1 Multicopper oxidases signature 1. GkWiIsSlTPkhLqAGMqayI
ChainResidueDetails
CGLY276-ILE296
DGLY1852-PHE1872

site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
BLEU232-CYS237
ELEU359-CYS364

site_idPS01186
Number of Residues12
DetailsEGF_2 EGF-like domain signature 2. CtCleGFegkn....C
ChainResidueDetails
ACYS70-CYS81
ACYS109-CYS124

site_idPS01187
Number of Residues25
DetailsEGF_CA Calcium-binding EGF-like domain signature. DgDQCetsp..........Cqnqgk..CkDglgeYtC
ChainResidueDetails
AASP46-CYS70

site_idPS01285
Number of Residues34
DetailsFA58C_1 Coagulation factors 5/8 type C domain (FA58C) signature 1. AWsveklaaefaskp..WIqVDmqkeviItgIqTQG
ChainResidueDetails
DALA1919-GLY1952
DALA2083-GLY2112

site_idPS01286
Number of Residues17
DetailsFA58C_2 Coagulation factors 5/8 type C domain (FA58C) signature 2. Ptraynrpt..LRlELqGC
ChainResidueDetails
DPRO2017-CYS2033
DPRO2177-CYS2193

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Charge relay system
ChainResidueDetails
BHIS236
AGLU32
AGLU39
BASP282
BALA379
AGLU16
AGLU19
AGLU20
AGLU25
AGLU26
AGLU29

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Sulfotyrosine => ECO:0000255
ChainResidueDetails
DTYR1565
CARG506
CARG679

site_idSWS_FT_FI3
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
DASN1675
DASN1982
DASN2181

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332
ChainResidueDetails
CTHR612
EGLU7

site_idSWS_FT_FI5
Number of Residues3
DetailsMOD_RES: Sulfotyrosine => ECO:0000255
ChainResidueDetails
CTYR665
CTYR696
CTYR698
EGLU20
EGLU25
EGLU26
EGLU29
EGLU32

site_idSWS_FT_FI6
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
CASN23
CASN27
CASN211
CASN354
CASN440
CASN526

site_idSWS_FT_FI7
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952
ChainResidueDetails
CASN269

site_idSWS_FT_FI8
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952
ChainResidueDetails
CASN432

222926

PDB entries from 2024-07-24

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