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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

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
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
E0007599biological_processhemostasis
E0008083molecular_functiongrowth factor activity
E0008201molecular_functionheparin binding
E0008233molecular_functionpeptidase activity
E0008236molecular_functionserine-type peptidase activity
E0009611biological_processresponse to wounding
E0009897cellular_componentexternal side of plasma membrane
E0010544biological_processnegative regulation of platelet activation
E0016787molecular_functionhydrolase activity
E0030168biological_processplatelet activation
E0030193biological_processregulation of blood coagulation
E0030194biological_processpositive regulation of blood coagulation
E0030195biological_processnegative regulation of blood coagulation
E0031012cellular_componentextracellular matrix
E0032967biological_processpositive regulation of collagen biosynthetic process
E0042730biological_processfibrinolysis
E0045861biological_processnegative regulation of proteolysis
E0046427biological_processpositive regulation of receptor signaling pathway via JAK-STAT
E0048018molecular_functionreceptor ligand activity
E0048712biological_processnegative regulation of astrocyte differentiation
E0050878biological_processregulation of body fluid levels
E0051281biological_processpositive regulation of release of sequestered calcium ion into cytosol
E0051480biological_processregulation of cytosolic calcium ion concentration
E0051918biological_processnegative regulation of fibrinolysis
E0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
E0070053molecular_functionthrombospondin receptor activity
E0070062cellular_componentextracellular exosome
E0070493biological_processthrombin-activated receptor signaling pathway
E0070945biological_processneutrophil-mediated killing of gram-negative bacterium
E0072562cellular_componentblood microparticle
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
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. GwWlLnTeVGenQrAGMqtpF
ChainResidueDetails
DGLY1852-PHE1872
CGLY276-ILE296
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 Residues154
DetailsPeptide: {"description":"Activation peptide fragment 1","featureId":"PRO_0000028161"}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues89
DetailsDomain: {"description":"Gla","evidences":[{"source":"PROSITE-ProRule","id":"PRU00463","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues78
DetailsDomain: {"description":"Kringle 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00121","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues486
DetailsDomain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues22
DetailsRegion: {"description":"High affinity receptor-binding region which is also known as the TP508 peptide"}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues6
DetailsActive site: {"description":"Charge relay system"}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsSite: {"description":"Cleavage; by thrombin"}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsSite: {"description":"Cleavage; by factor Xa","evidences":[{"source":"PubMed","id":"34265300","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
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_FI10
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_FI11
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_FI12
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
site_idSWS_FT_FI13
Number of Residues36
DetailsDomain: {"description":"EGF-like 1; calcium-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues40
DetailsDomain: {"description":"EGF-like 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI15
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_FI16
Number of Residues1
DetailsModified residue: {"description":"(3R)-3-hydroxyaspartate","evidences":[{"source":"PubMed","id":"6871167","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues299
DetailsDomain: {"description":"F5/8 type A 1"}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues163
DetailsDomain: {"description":"Plastocyanin-like 1"}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues126
DetailsDomain: {"description":"Plastocyanin-like 2"}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues336
DetailsDomain: {"description":"F5/8 type A 2"}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues178
DetailsDomain: {"description":"Plastocyanin-like 3"}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues148
DetailsDomain: {"description":"Plastocyanin-like 4"}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues4
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues3
DetailsSite: {"description":"Cleavage; by activated protein C","evidences":[{"source":"PubMed","id":"7989361","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues4
DetailsModified residue: {"description":"Sulfotyrosine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues9
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI28
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_FI29
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI30
Number of Residues146
DetailsDomain: {"description":"Plastocyanin-like 6"}
ChainResidueDetails
site_idSWS_FT_FI31
Number of Residues154
DetailsDomain: {"description":"F5/8 type C 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00081","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI32
Number of Residues155
DetailsDomain: {"description":"F5/8 type C 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00081","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI33
Number of Residues9
DetailsRegion: {"description":"O-glycosylated at one site"}
ChainResidueDetails

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PDB entries from 2026-01-14

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