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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9CTH

Preliminary map of the Prothrombin-prothrombinase complex on nano discs

This is a non-PDB format compatible entry.
Replaces:  7TPQ
Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
B0005509molecular_functioncalcium ion binding
B0005576cellular_componentextracellular region
C0004252molecular_functionserine-type endopeptidase activity
C0006508biological_processproteolysis
D0001530molecular_functionlipopolysaccharide binding
D0004175molecular_functionendopeptidase activity
D0004252molecular_functionserine-type endopeptidase activity
D0005102molecular_functionsignaling receptor binding
D0005509molecular_functioncalcium ion binding
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005615cellular_componentextracellular space
D0005788cellular_componentendoplasmic reticulum lumen
D0005796cellular_componentGolgi lumen
D0005886cellular_componentplasma membrane
D0006508biological_processproteolysis
D0006953biological_processacute-phase response
D0007166biological_processcell surface receptor signaling pathway
D0007186biological_processG protein-coupled receptor signaling pathway
D0007596biological_processblood coagulation
D0007599biological_processhemostasis
D0008083molecular_functiongrowth factor activity
D0008201molecular_functionheparin binding
D0008233molecular_functionpeptidase activity
D0008236molecular_functionserine-type peptidase activity
D0008284biological_processpositive regulation of cell population proliferation
D0008360biological_processregulation of cell shape
D0009611biological_processresponse to wounding
D0009897cellular_componentexternal side of plasma membrane
D0010468biological_processregulation of gene expression
D0010544biological_processnegative regulation of platelet activation
D0016787molecular_functionhydrolase activity
D0030168biological_processplatelet activation
D0030193biological_processregulation of blood coagulation
D0030194biological_processpositive regulation of blood coagulation
D0030195biological_processnegative regulation of blood coagulation
D0030307biological_processpositive regulation of cell growth
D0031012cellular_componentextracellular matrix
D0032024biological_processpositive regulation of insulin secretion
D0032967biological_processpositive regulation of collagen biosynthetic process
D0042730biological_processfibrinolysis
D0045861biological_processnegative regulation of proteolysis
D0046427biological_processpositive regulation of receptor signaling pathway via JAK-STAT
D0048018molecular_functionreceptor ligand activity
D0048712biological_processnegative regulation of astrocyte differentiation
D0050878biological_processregulation of body fluid levels
D0051281biological_processpositive regulation of release of sequestered calcium ion into cytosol
D0051480biological_processregulation of cytosolic calcium ion concentration
D0051838biological_processcytolysis by host of symbiont cells
D0051897biological_processpositive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
D0051918biological_processnegative regulation of fibrinolysis
D0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
D0070053molecular_functionthrombospondin receptor activity
D0070062cellular_componentextracellular exosome
D0070493biological_processthrombin-activated receptor signaling pathway
D0070945biological_processneutrophil-mediated killing of gram-negative bacterium
D0072562cellular_componentblood microparticle
D1900016biological_processnegative regulation of cytokine production involved in inflammatory response
D1900182biological_processpositive regulation of protein localization to nucleus
D1900738biological_processpositive regulation of phospholipase C-activating G protein-coupled receptor signaling pathway
D1990806biological_processligand-gated ion channel signaling pathway
D2000379biological_processpositive regulation of reactive oxygen species metabolic process
E0005507molecular_functioncopper ion binding
Functional Information from PROSITE/UniProt
site_idPS00010
Number of Residues12
DetailsASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CkDglgeYtCtC
ChainResidueDetails
BCYS61-CYS72
site_idPS00011
Number of Residues26
DetailsGLA_1 Vitamin K-dependent carboxylation domain. EcmEEtCsyeearEvfedsdktne.FW
ChainResidueDetails
BGLU16-TRP41
DGLU16-TRP41
site_idPS00021
Number of Residues14
DetailsKRINGLE_1 Kringle domain signature. FCRNpdssttgpWC
ChainResidueDetails
DPHE113-CYS126
DPHE218-CYS231
site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CtCleGfeGKnC
ChainResidueDetails
BCYS70-CYS81
site_idPS00079
Number of Residues21
DetailsMULTICOPPER_OXIDASE1 Multicopper oxidases signature 1. GkWiIsSlTPkhLqAGMqayI
ChainResidueDetails
AGLY276-ILE296
EGLY1852-PHE1872
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
CLEU53-CYS58
DLEU359-CYS364
site_idPS01186
Number of Residues12
DetailsEGF_2 EGF-like domain signature 2. CtCleGFegkn....C
ChainResidueDetails
BCYS70-CYS81
BCYS109-CYS124
site_idPS01187
Number of Residues25
DetailsEGF_CA Calcium-binding EGF-like domain signature. DgDQCetsp..........Cqnqgk..CkDglgeYtC
ChainResidueDetails
BASP46-CYS70
site_idPS01285
Number of Residues34
DetailsFA58C_1 Coagulation factors 5/8 type C domain (FA58C) signature 1. AWsveklaaefaskp..WIqVDmqkeviItgIqTQG
ChainResidueDetails
EALA1919-GLY1952
EALA2083-GLY2112
site_idPS01286
Number of Residues17
DetailsFA58C_2 Coagulation factors 5/8 type C domain (FA58C) signature 2. Ptraynrpt..LRlELqGC
ChainResidueDetails
EPRO2017-CYS2033
EPRO2177-CYS2193
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues299
DetailsDomain: {"description":"F5/8 type A 1"}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues163
DetailsDomain: {"description":"Plastocyanin-like 1"}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues126
DetailsDomain: {"description":"Plastocyanin-like 2"}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues336
DetailsDomain: {"description":"F5/8 type A 2"}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues178
DetailsDomain: {"description":"Plastocyanin-like 3"}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues148
DetailsDomain: {"description":"Plastocyanin-like 4"}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues4
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsSite: {"description":"Cleavage; by activated protein C","evidences":[{"source":"PubMed","id":"7989361","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues9
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16263699","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues329
DetailsDomain: {"description":"F5/8 type A 3"}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues173
DetailsDomain: {"description":"Plastocyanin-like 5"}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues146
DetailsDomain: {"description":"Plastocyanin-like 6"}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues154
DetailsDomain: {"description":"F5/8 type C 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00081","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues155
DetailsDomain: {"description":"F5/8 type C 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00081","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues1
DetailsModified residue: {"description":"Sulfotyrosine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues89
DetailsDomain: {"description":"Gla","evidences":[{"source":"PROSITE-ProRule","id":"PRU00463","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues36
DetailsDomain: {"description":"EGF-like 1; calcium-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues40
DetailsDomain: {"description":"EGF-like 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues11
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_FI23
Number of Residues1
DetailsModified residue: {"description":"(3R)-3-hydroxyaspartate","evidences":[{"source":"PubMed","id":"6871167","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues486
DetailsDomain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues6
DetailsActive site: {"description":"Charge relay system"}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues78
DetailsDomain: {"description":"Kringle 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00121","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues78
DetailsDomain: {"description":"Kringle 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00121","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues22
DetailsRegion: {"description":"High affinity receptor-binding region which is also known as the TP508 peptide"}
ChainResidueDetails
site_idSWS_FT_FI29
Number of Residues2
DetailsSite: {"description":"Cleavage; by factor Xa","evidences":[{"source":"PubMed","id":"34265300","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI30
Number of Residues2
DetailsModified residue: {"description":"4-carboxyglutamate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00463","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"3759958","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6305407","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI31
Number of Residues8
DetailsModified residue: {"description":"4-carboxyglutamate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00463","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"6305407","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI32
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_FI33
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

239803

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