Coagulation factor X
Details
- Name
- Coagulation factor X
- Synonyms
- 3.4.21.6
- Stuart factor
- Stuart-Prower factor
- Gene Name
- F10
- Organism
- Humans
- Amino acid sequence
>lcl|BSEQ0010204|Coagulation factor X MGRPLHLVLLSASLAGLLLLGESLFIRREQANNILARVTRANSFLEEMKKGHLERECMEE TCSYEEAREVFEDSDKTNEFWNKYKDGDQCETSPCQNQGKCKDGLGEYTCTCLEGFEGKN CELFTRKLCSLDNGDCDQFCHEEQNSVVCSCARGYTLADNGKACIPTGPYPCGKQTLERR KRSVAQATSSSGEAPDSITWKPYDAADLDPTENPFDLLDFNQTQPERGDNNLTRIVGGQE CKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRFKVRVGDRNTEQEEGGE AVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITFRMNVAPACLPERDWAESTLMTQKTGI VSGFGRTHEKGRQSTRLKMLEVPYVDRNSCKLSSSFIITQNMFCAGYDTKQEDACQGDSG GPHVTRFKDTYFVTGIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKTRGLPKAKSHAPE VITSSPLK
- Number of residues
- 488
- Molecular Weight
- 54731.255
- Theoretical pI
- 5.74
- GO Classification
- Functionscalcium ion binding / phospholipid binding / serine-type endopeptidase activityProcessesblood coagulation / blood coagulation, extrinsic pathway / blood coagulation, intrinsic pathway / cellular protein metabolic process / peptidyl-glutamic acid carboxylation / positive regulation of cell migration / positive regulation of protein kinase B signaling / post-translational protein modification / proteolysisComponentsendoplasmic reticulum lumen / extracellular region / extracellular space / Golgi lumen / intrinsic component of external side of plasma membrane / plasma membrane
- General Function
- Serine-type endopeptidase activity
- Specific Function
- Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting.
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Secreted
- Gene sequence
>lcl|BSEQ0010205|Coagulation factor X (F10) ATGGGGCGCCCACTGCACCTCGTCCTGCTCAGTGCCTCCCTGGCTGGCCTCCTGCTGCTC GGGGAAAGTCTGTTCATCCGCAGGGAGCAGGCCAACAACATCCTGGCGAGGGTCACGAGG GCCAATTCCTTTCTTGAAGAGATGAAGAAAGGACACCTCGAAAGAGAGTGCATGGAAGAG ACCTGCTCATACGAAGAGGCCCGCGAGGTCTTTGAGGACAGCGACAAGACGAATGAATTC TGGAATAAATACAAAGATGGCGACCAGTGTGAGACCAGTCCTTGCCAGAACCAGGGCAAA TGTAAAGACGGCCTCGGGGAATACACCTGCACCTGTTTAGAAGGATTCGAAGGCAAAAAC TGTGAATTATTCACACGGAAGCTCTGCAGCCTGGACAACGGGGACTGTGACCAGTTCTGC CACGAGGAACAGAACTCTGTGGTGTGCTCCTGCGCCCGCGGGTACACCCTGGCTGACAAC GGCAAGGCCTGCATTCCCACAGGGCCCTACCCCTGTGGGAAACAGACCCTGGAACGCAGG AAGAGGTCAGTGGCCCAGGCCACCAGCAGCAGCGGGGAGGCCCCTGACAGCATCACATGG AAGCCATATGATGCAGCCGACCTGGACCCCACCGAGAACCCCTTCGACCTGCTTGACTTC AACCAGACGCAGCCTGAGAGGGGCGACAACAACCTCACCAGGATCGTGGGAGGCCAGGAA TGCAAGGACGGGGAGTGTCCCTGGCAGGCCCTGCTCATCAATGAGGAAAACGAGGGTTTC TGTGGTGGAACCATTCTGAGCGAGTTCTACATCCTAACGGCAGCCCACTGTCTCTACCAA GCCAAGAGATTCAAGGTGAGGGTAGGGGACCGGAACACGGAGCAGGAGGAGGGCGGTGAG GCGGTGCACGAGGTGGAGGTGGTCATCAAGCACAACCGGTTCACAAAGGAGACCTATGAC TTCGACATCGCCGTGCTCCGGCTCAAGACCCCCATCACCTTCCGCATGAACGTGGCGCCT GCCTGCCTCCCCGAGCGTGACTGGGCCGAGTCCACGCTGATGACGCAGAAGACGGGGATT GTGAGCGGCTTCGGGCGCACCCACGAGAAGGGCCGGCAGTCCACCAGGCTCAAGATGCTG GAGGTGCCCTACGTGGACCGCAACAGCTGCAAGCTGTCCAGCAGCTTCATCATCACCCAG AACATGTTCTGTGCCGGCTACGACACCAAGCAGGAGGATGCCTGCCAGGGGGACAGCGGG GGCCCGCACGTCACCCGCTTCAAGGACACCTACTTCGTGACAGGCATCGTCAGCTGGGGA GAGGGCTGTGCCCGTAAGGGGAAGTACGGGATCTACACCAAGGTCACCGCCTTCCTCAAG TGGATCGACAGGTCCATGAAAACCAGGGGCTTGCCCAAGGCCAAGAGCCATGCCCCGGAG GTCATAACGTCCTCTCCATTAAAGTGA
- Chromosome Location
- 13
- Locus
- 13q34
- External Identifiers
Resource Link UniProtKB ID P00742 UniProtKB Entry Name FA10_HUMAN GenBank Protein ID 182841 GenBank Gene ID K03194 GenAtlas ID F10 HGNC ID HGNC:3528 - General References
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- Fung MR, Hay CW, MacGillivray RT: Characterization of an almost full-length cDNA coding for human blood coagulation factor X. Proc Natl Acad Sci U S A. 1985 Jun;82(11):3591-5. [Article]
- Kaul RK, Hildebrand B, Roberts S, Jagadeeswaran P: Isolation and characterization of human blood-coagulation factor X cDNA. Gene. 1986;41(2-3):311-4. [Article]
- McMullen BA, Fujikawa K, Kisiel W, Sasagawa T, Howald WN, Kwa EY, Weinstein B: Complete amino acid sequence of the light chain of human blood coagulation factor X: evidence for identification of residue 63 as beta-hydroxyaspartic acid. Biochemistry. 1983 Jun 7;22(12):2875-84. [Article]
- Leytus SP, Chung DW, Kisiel W, Kurachi K, Davie EW: Characterization of a cDNA coding for human factor X. Proc Natl Acad Sci U S A. 1984 Jun;81(12):3699-702. [Article]
- Inoue K, Morita T: Identification of O-linked oligosaccharide chains in the activation peptides of blood coagulation factor X. The role of the carbohydrate moieties in the activation of factor X. Eur J Biochem. 1993 Nov 15;218(1):153-63. [Article]
- Jagadeeswaran P, Reddy SV, Rao KJ, Hamsabhushanam K, Lyman G: Cloning and characterization of the 5' end (exon 1) of the gene encoding human factor X. Gene. 1989 Dec 14;84(2):517-9. [Article]
- Suzuki K, Nishioka J, Kusumoto H, Hashimoto S: Mechanism of inhibition of activated protein C by protein C inhibitor. J Biochem. 1984 Jan;95(1):187-95. [Article]
- Huang X, Dementiev A, Olson ST, Gettins PG: Basis for the specificity and activation of the serpin protein Z-dependent proteinase inhibitor (ZPI) as an inhibitor of membrane-associated factor Xa. J Biol Chem. 2010 Jun 25;285(26):20399-409. doi: 10.1074/jbc.M110.112748. Epub 2010 Apr 28. [Article]
- Halim A, Nilsson J, Ruetschi U, Hesse C, Larson G: Human urinary glycoproteomics; attachment site specific analysis of N- and O-linked glycosylations by CID and ECD. Mol Cell Proteomics. 2012 Apr;11(4):M111.013649. doi: 10.1074/mcp.M111.013649. Epub 2011 Dec 14. [Article]
- Padmanabhan K, Padmanabhan KP, Tulinsky A, Park CH, Bode W, Huber R, Blankenship DT, Cardin AD, Kisiel W: Structure of human des(1-45) factor Xa at 2.2 A resolution. J Mol Biol. 1993 Aug 5;232(3):947-66. [Article]
- Kamata K, Kawamoto H, Honma T, Iwama T, Kim SH: Structural basis for chemical inhibition of human blood coagulation factor Xa. Proc Natl Acad Sci U S A. 1998 Jun 9;95(12):6630-5. [Article]
- Kochanny MJ, Adler M, Ewing J, Griedel BD, Ho E, Karanjawala R, Lee W, Lentz D, Liang AM, Morrissey MM, Phillips GB, Post J, Sacchi KL, Sakata ST, Subramanyam B, Vergona R, Walters J, White KA, Whitlow M, Ye B, Zhao Z, Shaw KJ: Substituted thiophene-anthranilamides as potent inhibitors of human factor Xa. Bioorg Med Chem. 2007 Mar 1;15(5):2127-46. Epub 2006 Dec 13. [Article]
- Reddy SV, Zhou ZQ, Rao KJ, Scott JP, Watzke H, High KA, Jagadeeswaran P: Molecular characterization of human factor XSan Antonio. Blood. 1989 Oct;74(5):1486-90. [Article]
- Watzke HH, Lechner K, Roberts HR, Reddy SV, Welsch DJ, Friedman P, Mahr G, Jagadeeswaran P, Monroe DM, High KA: Molecular defect (Gla+14----Lys) and its functional consequences in a hereditary factor X deficiency (factor X "Vorarlberg"). J Biol Chem. 1990 Jul 15;265(20):11982-9. [Article]
- James HL, Girolami A, Fair DS: Molecular defect in coagulation factor XFriuli results from a substitution of serine for proline at position 343. Blood. 1991 Jan 15;77(2):317-23. [Article]
- Marchetti G, Castaman G, Pinotti M, Lunghi B, Di Iasio MG, Ruggieri M, Rodeghiero F, Bernardi F: Molecular bases of CRM+ factor X deficiency: a frequent mutation (Ser334Pro) in the catalytic domain and a substitution (Glu102Lys) in the second EGF-like domain. Br J Haematol. 1995 Aug;90(4):910-5. [Article]
- Bezeaud A, Miyata T, Helley D, Zeng YZ, Kato H, Aillaud MF, Juhan-Vague I, Guillin MC: Functional consequences of the Ser334-->Pro mutation in a human factor X variant (factor XMarseille). Eur J Biochem. 1995 Nov 15;234(1):140-7. [Article]
- Kim DJ, Thompson AR, James HL: Factor XKetchikan: a variant molecule in which Gly replaces a Gla residue at position 14 in the light chain. Hum Genet. 1995 Feb;95(2):212-4. [Article]
- Messier TL, Wong CY, Bovill EG, Long GL, Church WR: Factor X Stockton: a mild bleeding diathesis associated with an active site mutation in factor X. Blood Coagul Fibrinolysis. 1996 Jan;7(1):5-14. [Article]
- Rudolph AE, Mullane MP, Porche-Sorbet R, Tsuda S, Miletich JP: Factor XSt. Louis II. Identification of a glycine substitution at residue 7 and characterization of the recombinant protein. J Biol Chem. 1996 Nov 8;271(45):28601-6. [Article]
- Zama T, Murata M, Watanabe R, Yokoyama K, Moriki T, Ambo H, Murakami H, Kikuchi M, Ikeda Y: A family with hereditary factor X deficiency with a point mutation Gla32 to Gln in the Gla domain (factor X Tokyo). Br J Haematol. 1999 Sep;106(3):809-11. [Article]
- Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [Article]
- Millar DS, Elliston L, Deex P, Krawczak M, Wacey AI, Reynaud J, Nieuwenhuis HK, Bolton-Maggs P, Mannucci PM, Reverter JC, Cachia P, Pasi KJ, Layton DM, Cooper DN: Molecular analysis of the genotype-phenotype relationship in factor X deficiency. Hum Genet. 2000 Feb;106(2):249-57. [Article]
- Forberg E, Huhmann I, Jimenez-Boj E, Watzke HH: The impact of Glu102Lys on the factor X function in a patient with a doubly homozygous factor X deficiency (Gla14Lys and Glu102Lys). Thromb Haemost. 2000 Feb;83(2):234-8. [Article]
- Simioni P, Vianello F, Kalafatis M, Barzon L, Ladogana S, Paolucci P, Carotenuto M, Dal Bello F, Palu G, Girolami A: A dysfunctional factor X (factor X San Giovanni Rotondo) present at homozygous and double heterozygous level: identification of a novel microdeletion (delC556) and missense mutation (Lys(408)-->Asn) in the factor X gene. A study of an Italian family. Thromb Res. 2001 Feb 15;101(4):219-30. [Article]
- Vianello F, Lombardi AM, Boldrin C, Luni S, Girolami A: A new factor X defect (factor X Padua 3): a compound heterozygous between true deficiency (Gly(380)-->Arg) and an abnormality (Ser(334)-->Pro). Thromb Res. 2001 Nov 15;104(4):257-64. [Article]
- Vianello F, Lombardi AM, Bello FD, Palu G, Zanon E, Girolami A: A novel type I factor X variant (factor X Cys350Phe) due to loss of a disulfide bond in the catalytic domain. Blood Coagul Fibrinolysis. 2003 Jun;14(4):401-5. [Article]
- Pinotti M, Camire RM, Baroni M, Rajab A, Marchetti G, Bernardi F: Impaired prothrombinase activity of factor X Gly381Asp results in severe familial CRM+ FX deficiency. Thromb Haemost. 2003 Feb;89(2):243-8. [Article]
- Pinotti M, Monti M, Baroni M, Marchetti G, Bernardi F: Molecular characterization of factor X deficiency associated with borderline plasma factor X level. Haematologica. 2004 Apr;89(4):501-2. [Article]
- Isshiki I, Favier R, Moriki T, Uchida T, Ishihara H, Van Dreden P, Murata M, Ikeda Y: Genetic analysis of hereditary factor X deficiency in a French patient of Sri Lankan ancestry: in vitro expression study identified Gly366Ser substitution as the molecular basis of the dysfunctional factor X. Blood Coagul Fibrinolysis. 2005 Jan;16(1):9-16. [Article]
- Al-Hilali A, Wulff K, Abdel-Razeq H, Saud KA, Al-Gaili F, Herrmann FH: Analysis of the novel factor X gene mutation Glu51Lys in two families with factor X-Riyadh anomaly. Thromb Haemost. 2007 Apr;97(4):542-5. [Article]
- Chafa O, Tagzirt M, Tapon-Bretaudiere J, Reghis A, Fischer AM, LeBonniec BF: Characterization of a homozygous Gly11Val mutation in the Gla domain of coagulation factor X. Thromb Res. 2009 May;124(1):144-8. doi: 10.1016/j.thromres.2008.11.018. Epub 2009 Jan 10. [Article]
- Abdel-Azeim S, Oliva R, Chermak E, De Cristofaro R, Cavallo L: Molecular dynamics characterization of five pathogenic Factor X mutants associated with decreased catalytic activity. Biochemistry. 2014 Nov 11;53(44):6992-7001. doi: 10.1021/bi500770p. Epub 2014 Oct 24. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB00025 Antihemophilic factor, human recombinant approved, investigational yes activator Details DB00100 Coagulation Factor IX (Recombinant) approved, investigational yes activator Details DB00036 Coagulation factor VIIa Recombinant Human approved unknown Details DB01109 Heparin approved, investigational yes inhibitor Details DB01225 Enoxaparin approved yes inhibitor Details DB05362 SSR-126517E investigational unknown Details DB03847 gamma-carboxy-L-glutamic acid experimental unknown Details DB04673 4-[(5-CHLOROINDOL-2-YL)SULFONYL]-2-(2-METHYLPROPYL)-1-[[5-(PYRIDIN-4-YL)PYRIMIDIN-2-YL]CARBONYL]PIPERAZINE experimental unknown Details DB05713 LY-517717 investigational unknown Details DB06228 Rivaroxaban approved yes antagonist Details DB06245 Lanoteplase investigational unknown Details DB06406 Idraparinux investigational unknown Details DB06552 rNAPc2 investigational unknown Details DB06605 Apixaban approved yes inhibitor Details DB06635 Otamixaban investigational unknown Details DB06920 Eribaxaban experimental unknown Details DB07211 (2R)-2-(5-CHLORO-2-THIENYL)-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}PROPENE-1-SULFONAMIDE experimental unknown Details DB07261 THIENO[3,2-B]PYRIDINE-2-SULFONIC ACID [1-(1-AMINO-ISOQUINOLIN-7-YLMETHYL)-2-OXO-PYRROLDIN-3-YL]-AMIDE experimental unknown Details DB07277 2-(5-CHLORO-2-THIENYL)-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}ETHANESULFONAMIDE experimental unknown Details DB07278 GW-813893 experimental unknown Details DB07605 2-({4-[(5-CHLORO-1H-INDOL-2-YL)SULFONYL]PIPERAZIN-1-YL}CARBONYL)THIENO[3,2-B]PYRIDINE 4-OXIDE experimental unknown Details DB07629 N-((1R,2S)-2-(5-CHLORO-1H-INDOLE-2-CARBOXAMIDO)CYCLOHEXYL)-5-METHYL-4,5,6,7-TETRAHYDROTHIAZOLO[5,4-C]PYRIDINE-2-CARBOXAMIDE experimental unknown Details DB07630 N-((1R,2R)-2-(5-CHLORO-1H-INDOLE-2-CARBOXAMIDO)CYCLOHEXYL)-5-METHYL-4,5,6,7-TETRAHYDROTHIAZOLO[5,4-C]PYRIDINE-2-CARBOXAMIDE experimental unknown Details DB07800 N-(2-(((5-CHLORO-2-PYRIDINYL)AMINO)SULFONYL)PHENYL)-4-(2-OXO-1(2H)-PYRIDINYL)BENZAMIDE experimental unknown Details DB07804 5-(5-CHLORO-2-THIENYL)-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}-1H-1,2,4-TRIAZOLE-3-SULFONAMIDE experimental unknown Details DB07843 5-CHLORO-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}-1-BENZOTHIOPHENE-2-SULFONAMIDE experimental unknown Details DB07844 6-CHLORO-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}-1-BENZOTHIOPHENE-2-SULFONAMIDE experimental unknown Details DB07847 6-CHLORO-N-{(3S)-1-[(1S)-1-METHYL-2-(4-MORPHOLINYL)-2-OXO ETHYL]-2-OXO-3-PYRROLIDINYL}-2-NAPHTHALENESULFONAMIDE experimental unknown Details DB07848 5-Chloro-N-{(3S)-1-[(2S)-1-(4-morpholinyl)-1-oxo-2-propanyl]-2-oxo-3-pyrrolidinyl}-1H-indole-2-sulfonamide experimental unknown Details DB07872 5-chloro-N-[(3R)-1-(2-{[2-fluoro-4-(2-oxopyridin-1(2H)-yl)phenyl]amino}-2-oxoethyl)pyrrolidin-3-yl]thiophene-2-carboxamide experimental unknown Details DB07875 5-Chloro-thiophene-2-carboxylic acid ((3S,4S)-1-{[2-fluoro-4-(2-oxo-2H-pyridin-1-yl)-phenylcarbamoyl]-methyl}-4-hydroxy-pyrrolidin-3-yl)-amide experimental unknown Details DB07973 N-(1-ISOPROPYLPIPERIDIN-4-YL)-1-(3-METHOXYBENZYL)-1H-INDOLE-2-CARBOXAMIDE experimental unknown Details DB07974 1-{2-[(4-CHLOROPHENYL)AMINO]-2-OXOETHYL}-N-(1-ISOPROPYLPIPERIDIN-4-YL)-1H-INDOLE-2-CARBOXAMIDE experimental unknown Details DB08143 5-CHLORO-THIOPHENE-2-CARBOXYLIC ACID ((3S,4S)-4-FLUORO- 1-{[2-FLUORO-4-(2-OXO-2H-PYRIDIN-1-YL)-PHENYLCARBAMOYL]-METHYL}-PYRROLIDIN-3-YL)-AMIDE experimental unknown Details DB08173 5-CHLORO-N-(2-(4-(2-OXOPYRIDIN-1(2H)-YL)BENZAMIDO)ETHYL)THIOPHENE-2-CARBOXAMIDE experimental unknown Details DB08174 5-CHLORO-N-((1R,2S)-2-(4-(2-OXOPYRIDIN-1(2H)-YL)BENZAMIDO) CYCLOPENTYL)THIOPHENE-2-CARBOXAMIDE experimental unknown Details DB08426 THIENO[3,2-B]PYRIDINE-2-SULFONIC ACID [2-OXO-1-(1H-PYRROLO[2,3-C]PYRIDIN-2-YLMETHYL)-PYRROLIDIN-3-YL]-AMIDE experimental unknown Details DB08487 3-({4-[(6-CHLORO-1-BENZOTHIEN-2-YL)SULFONYL]-2-OXOPIPERAZIN-1-YL}METHYL)BENZENECARBOXIMIDAMIDE experimental unknown Details DB08488 4-{[(E)-2-(5-CHLOROTHIEN-2-YL)VINYL]SULFONYL}-1-(1H-PYRROLO[3,2-C]PYRIDIN-2-YLMETHYL)PIPERAZIN-2-ONE experimental unknown Details DB08495 4-({4-[(6-CHLORO-1-BENZOTHIEN-2-YL)SULFONYL]-2-OXOPIPERAZIN-1-YL}METHYL)BENZENECARBOXIMIDAMIDE experimental unknown Details DB08745 4-[[(1E)-2-(4-CHLOROPHENYL)ETHENYL]SULFONYL]-1-[[1-(4-PYRIDINYL)-4-PIPERIDINYL]METHYL]PIPERAZINONE experimental unknown Details DB08746 1-[[(1E)-2-(4-CHLOROPHENYL)ETHENYL]SULFONYL]-4-[[1-(4-PYRIDINYL)-4-PIPERIDINYL]METHYL]PIPERAZINE experimental unknown Details DB00569 Fondaparinux approved, investigational yes inhibitor Details DB09075 Edoxaban approved yes inhibitor Details DB13150 Coagulation factor VII human approved, investigational yes activator Details DB11166 Antithrombin Alfa approved, investigational yes inhibitor Details DB12598 Nafamostat investigational yes inhibitor Details DB13152 Coagulation Factor IX Human approved yes activator Details DB11311 Prothrombin approved no substrate Details DB13149 Protein S human approved yes antagonist Details DB13151 Anti-inhibitor coagulant complex approved, investigational yes agonist Details DB12364 Betrixaban approved, investigational yes inhibitor Details DB13923 Emicizumab approved, investigational yes activator Details DB13192 Antihemophilic factor human approved yes activator Details DB13933 Nonacog beta pegol approved, investigational yes agonist Details DB09109 Turoctocog alfa approved, investigational yes activator Details DB09258 Bemiparin approved, investigational yes antagonist Details DB09332 Kappadione approved unknown agonist Details DB13998 Lonoctocog alfa approved, investigational yes activator Details DB13999 Moroctocog alfa approved yes activator Details DB13884 Albutrepenonacog alfa approved yes activator Details DB09141 Protamine sulfate approved unknown Details DB14738 Turoctocog alfa pegol approved unknown substrate Details DB14738 Turoctocog alfa pegol approved yes activator Details DB16662 Efanesoctocog alfa approved, investigational unknown binder Details