1lqd - Revision history

OCA at 08:26, 10 April 2024

OCA — Wed, 10 Apr 2024 08:26:16 GMT

←Older revision		Revision as of 08:26, 10 April 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1lqd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LQD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LQD FirstGlance]. <br>		<table><tr><td colspan='2'>[[1lqd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LQD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LQD FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>~~, ~~<scene name='pdbligand=CMI:1-(3-CARBAMIMIDOYL-BENZYL)-4-METHYL-1H-INDOLE-~~2~~-CARBOXYLIC+ACID+3,5-DIMETHYL-BENZYLAMIDE'>CMI</scene>~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.7Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height: 3em;~~'>~~[[1lpg\|1lpg]], [[1lpk\|1lpk]], [[1lpz\|1lpz]], [[1lqe\|1lqe]]~~</~~div~~><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CMI:1-(3-CARBAMIMIDOYL-BENZYL)-4-METHYL-1H-INDOLE-2-CARBOXYLIC+ACID+3,5-DIMETHYL-BENZYLAMIDE'>CMI</scene></td></tr>
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Coagulation_factor_Xa Coagulation factor Xa], with EC number [https://www.brenda~~-~~enzymes.info/php/result_flat.php4?ecno=~~3.4~~.21.6~~ 3~~.4.21.6]~~ </~~span~~></td></tr>	+
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lqd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lqd OCA], [https://pdbe.org/1lqd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lqd RCSB], [https://www.ebi.ac.uk/pdbsum/1lqd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lqd ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lqd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lqd OCA], [https://pdbe.org/1lqd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lqd RCSB], [https://www.ebi.ac.uk/pdbsum/1lqd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lqd ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/FA10_HUMAN FA10_HUMAN]] Defects in F10 are the cause of factor X deficiency (FA10D) [MIM:[https://omim.org/entry/227600 227600]]. A hemorrhagic disease with variable presentation. Affected individuals can manifest prolonged nasal and mucosal hemorrhage, menorrhagia, hematuria, and occasionally hemarthrosis. Some patients do not have clinical bleeding diathesis.<ref>PMID:2790181</ref> <ref>PMID:1973167</ref> <ref>PMID:1985698</ref> <ref>PMID:7669671</ref> <ref>PMID:8529633</ref> <ref>PMID:7860069</ref> <ref>PMID:8845463</ref> <ref>PMID:8910490</ref> <ref>PMID:10468877</ref> <ref>PMID:10746568</ref> <ref>PMID:10739379</ref> <ref>PMID:11248282</ref> <ref>PMID:11728527</ref> <ref>PMID:12945883</ref> <ref>PMID:15650540</ref> <ref>PMID:17393015</ref> <ref>PMID:19135706</ref>	+	[https://www.uniprot.org/uniprot/FA10_HUMAN FA10_HUMAN] Defects in F10 are the cause of factor X deficiency (FA10D) [MIM:[https://omim.org/entry/227600 227600]. A hemorrhagic disease with variable presentation. Affected individuals can manifest prolonged nasal and mucosal hemorrhage, menorrhagia, hematuria, and occasionally hemarthrosis. Some patients do not have clinical bleeding diathesis.<ref>PMID:2790181</ref> <ref>PMID:1973167</ref> <ref>PMID:1985698</ref> <ref>PMID:7669671</ref> <ref>PMID:8529633</ref> <ref>PMID:7860069</ref> <ref>PMID:8845463</ref> <ref>PMID:8910490</ref> <ref>PMID:10468877</ref> <ref>PMID:10746568</ref> <ref>PMID:10739379</ref> <ref>PMID:11248282</ref> <ref>PMID:11728527</ref> <ref>PMID:12945883</ref> <ref>PMID:15650540</ref> <ref>PMID:17393015</ref> <ref>PMID:19135706</ref>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/FA10_HUMAN FA10_HUMAN]] 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.	+	[https://www.uniprot.org/uniprot/FA10_HUMAN FA10_HUMAN] 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.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1lqd ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1lqd ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	A series of 138 nonchiral 3-amidinobenzyl-1H-indole-2-carboxamides and analogues as inhibitors of the blood coagulation enzyme factor Xa (fXa) were designed, synthesized, and investigated by X-ray structure analysis and 3D quantitative structure-activity relationship (QSAR) studies (CoMFA, CoMSIA) in order to identify important protein-ligand interactions responsible for biological affinity and selectivity. Several compounds from this series are highly potent and selective inhibitors of this important enzyme linking extrinsic and intrinsic coagulation pathways. To rationalize biological affinity and to provide guidelines for further design, all compounds were docked into the factor Xa binding site. Those docking studies were based on X-ray structures of factor Xa in complex with literature-known inhibitors. It was possible to validate those binding modes by four X-ray crystal structures of representative ligands in factor Xa, while one ligand was additionally crystallized in trypsin to rationalize requirements for selective factor Xa inhibition. The 3D-QSAR models based on a superposition rule derived from these docking studies were validated using conventional and cross-validated r(2) values using the leave-one-out method and repeated analyses using two randomly chosen cross-validation groups plus randomization of biological activities. This led to consistent and highly predictive 3D-QSAR models with good correlation coefficients for both CoMFA and CoMSIA, which were found to correspond to experimentally determined factor Xa binding site topology in terms of steric, electrostatic, and hydrophobic complementarity. Subsets selected as smaller training sets using 2D fingerprints and maximum dissimilarity methods resulted in 3D-QSAR models with remarkable correlation coefficients and a high predictive power. The final quantitative SAR information agrees with all experimental data for the binding topology and thus provides reasonable activity predictions for novel factor Xa inhibitors.
-
-	Design and quantitative structure-activity relationship of 3-amidinobenzyl-1H-indole-2-carboxamides as potent, nonchiral, and selective inhibitors of blood coagulation factor Xa.,Matter H, Defossa E, Heinelt U, Blohm PM, Schneider D, Muller A, Herok S, Schreuder H, Liesum A, Brachvogel V, Lonze P, Walser A, Al-Obeidi F, Wildgoose P J Med Chem. 2002 Jun 20;45(13):2749-69. PMID:12061878<ref>PMID:12061878</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1lqd" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Coagulation factor Xa]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Brachvogel, V]]	+	[[Category: Brachvogel V]]
-	[[Category: Liesum, A]]	+	[[Category: Liesum A]]
-	[[Category: Loenze, P]]	+	[[Category: Loenze P]]
-	[[Category: Schreuder~~, H A]]~~	+	[[Category: Schreuder HA]]
-	~~[[Category: Blood coagulation factor]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Protein-inhibitor complex]]~~	+
-	~~[[Category: Serine proteinase~~]]	+

OCA at 06:48, 18 August 2021

OCA — Wed, 18 Aug 2021 06:48:08 GMT

OCA at 12:24, 13 November 2019

OCA — Wed, 13 Nov 2019 12:24:42 GMT

←Older revision		Revision as of 12:24, 13 November 2019
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	==CRYSTAL STRUCTURE OF FXA IN COMPLEX WITH 45.==		==CRYSTAL STRUCTURE OF FXA IN COMPLEX WITH 45.==
-	<StructureSection load='1lqd' size='340' side='right' caption='[[1lqd]], [[Resolution\|resolution]] 2.70Å' scene=''>	+	<StructureSection load='1lqd' size='340' side='right'caption='[[1lqd]], [[Resolution\|resolution]] 2.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1lqd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LQD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LQD FirstGlance]. <br>		<table><tr><td colspan='2'>[[1lqd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LQD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LQD FirstGlance]. <br>
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	</div>		</div>
	<div class="pdbe-citations 1lqd" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1lqd" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Factor Xa\|Factor Xa]]
	== References ==		== References ==
	<references/>		<references/>
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	[[Category: Coagulation factor Xa]]		[[Category: Coagulation factor Xa]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
		+	[[Category: Large Structures]]
	[[Category: Brachvogel, V]]		[[Category: Brachvogel, V]]
	[[Category: Liesum, A]]		[[Category: Liesum, A]]

OCA at 08:00, 31 January 2018

OCA — Wed, 31 Jan 2018 08:00:07 GMT

←Older revision		Revision as of 08:00, 31 January 2018
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		+
	==CRYSTAL STRUCTURE OF FXA IN COMPLEX WITH 45.==		==CRYSTAL STRUCTURE OF FXA IN COMPLEX WITH 45.==
	<StructureSection load='1lqd' size='340' side='right' caption='[[1lqd]], [[Resolution\|resolution]] 2.70Å' scene=''>		<StructureSection load='1lqd' size='340' side='right' caption='[[1lqd]], [[Resolution\|resolution]] 2.70Å' scene=''>
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	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1lpg\|1lpg]], [[1lpk\|1lpk]], [[1lpz\|1lpz]], [[1lqe\|1lqe]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1lpg\|1lpg]], [[1lpk\|1lpk]], [[1lpz\|1lpz]], [[1lqe\|1lqe]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Coagulation_factor_Xa Coagulation factor Xa], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.6 3.4.21.6] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Coagulation_factor_Xa Coagulation factor Xa], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.6 3.4.21.6] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lqd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lqd OCA], [http://pdbe.org/1lqd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lqd RCSB], [http://www.ebi.ac.uk/pdbsum/1lqd PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lqd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lqd OCA], [http://pdbe.org/1lqd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lqd RCSB], [http://www.ebi.ac.uk/pdbsum/1lqd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1lqd ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lq/1lqd_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lq/1lqd_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
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	</div>		</div>
	<div class="pdbe-citations 1lqd" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1lqd" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Factor Xa\|Factor Xa]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 09:12, 7 February 2016

OCA — Sun, 07 Feb 2016 09:12:06 GMT

←Older revision		Revision as of 09:12, 7 February 2016
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	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1lqd ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 23:56, 9 September 2015

OCA — Wed, 09 Sep 2015 23:56:06 GMT

←Older revision		Revision as of 23:56, 9 September 2015
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	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1lpg\|1lpg]], [[1lpk\|1lpk]], [[1lpz\|1lpz]], [[1lqe\|1lqe]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1lpg\|1lpg]], [[1lpk\|1lpk]], [[1lpz\|1lpz]], [[1lqe\|1lqe]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Coagulation_factor_Xa Coagulation factor Xa], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.6 3.4.21.6] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Coagulation_factor_Xa Coagulation factor Xa], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.6 3.4.21.6] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lqd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lqd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1lqd RCSB], [http://www.ebi.ac.uk/pdbsum/1lqd PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lqd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lqd OCA], [http://pdbe.org/1lqd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lqd RCSB], [http://www.ebi.ac.uk/pdbsum/1lqd PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
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	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 1lqd" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 16:48, 5 January 2015

OCA — Mon, 05 Jan 2015 16:48:55 GMT

←Older revision		Revision as of 16:48, 5 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1lqd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LQD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LQD FirstGlance]. <br>		<table><tr><td colspan='2'>[[1lqd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LQD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LQD FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CMI:1-(3-CARBAMIMIDOYL-BENZYL)-4-METHYL-1H-INDOLE-2-CARBOXYLIC+ACID+3,5-DIMETHYL-BENZYLAMIDE'>CMI</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CMI:1-(3-CARBAMIMIDOYL-BENZYL)-4-METHYL-1H-INDOLE-2-CARBOXYLIC+ACID+3,5-DIMETHYL-BENZYLAMIDE'>CMI</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1lpg\|1lpg]], [[1lpk\|1lpk]], [[1lpz\|1lpz]], [[1lqe\|1lqe]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1lpg\|1lpg]], [[1lpk\|1lpk]], [[1lpz\|1lpz]], [[1lqe\|1lqe]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Coagulation_factor_Xa Coagulation factor Xa], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.6 3.4.21.6] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Coagulation_factor_Xa Coagulation factor Xa], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.6 3.4.21.6] </span></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lqd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lqd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1lqd RCSB], [http://www.ebi.ac.uk/pdbsum/1lqd PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lqd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lqd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1lqd RCSB], [http://www.ebi.ac.uk/pdbsum/1lqd PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/FA10_HUMAN FA10_HUMAN]] Defects in F10 are the cause of factor X deficiency (FA10D) [MIM:[http://omim.org/entry/227600 227600]]. A hemorrhagic disease with variable presentation. Affected individuals can manifest prolonged nasal and mucosal hemorrhage, menorrhagia, hematuria, and occasionally hemarthrosis. Some patients do not have clinical bleeding diathesis.<ref>PMID:2790181</ref> <ref>PMID:1973167</ref> <ref>PMID:1985698</ref> <ref>PMID:7669671</ref> <ref>PMID:8529633</ref> <ref>PMID:7860069</ref> <ref>PMID:8845463</ref> <ref>PMID:8910490</ref> <ref>PMID:10468877</ref> <ref>PMID:10746568</ref> <ref>PMID:10739379</ref> <ref>PMID:11248282</ref> <ref>PMID:11728527</ref> <ref>PMID:12945883</ref> <ref>PMID:15650540</ref> <ref>PMID:17393015</ref> <ref>PMID:19135706</ref>		[[http://www.uniprot.org/uniprot/FA10_HUMAN FA10_HUMAN]] Defects in F10 are the cause of factor X deficiency (FA10D) [MIM:[http://omim.org/entry/227600 227600]]. A hemorrhagic disease with variable presentation. Affected individuals can manifest prolonged nasal and mucosal hemorrhage, menorrhagia, hematuria, and occasionally hemarthrosis. Some patients do not have clinical bleeding diathesis.<ref>PMID:2790181</ref> <ref>PMID:1973167</ref> <ref>PMID:1985698</ref> <ref>PMID:7669671</ref> <ref>PMID:8529633</ref> <ref>PMID:7860069</ref> <ref>PMID:8845463</ref> <ref>PMID:8910490</ref> <ref>PMID:10468877</ref> <ref>PMID:10746568</ref> <ref>PMID:10739379</ref> <ref>PMID:11248282</ref> <ref>PMID:11728527</ref> <ref>PMID:12945883</ref> <ref>PMID:15650540</ref> <ref>PMID:17393015</ref> <ref>PMID:19135706</ref>
Line 39:		Line 39:
	[[Category: Coagulation factor Xa]]		[[Category: Coagulation factor Xa]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Brachvogel, V.]]	+	[[Category: Brachvogel, V]]
-	[[Category: Liesum, A.]]	+	[[Category: Liesum, A]]
-	[[Category: Loenze, P.]]	+	[[Category: Loenze, P]]
-	[[Category: Schreuder, H A.]]	+	[[Category: Schreuder, H A]]
	[[Category: Blood coagulation factor]]		[[Category: Blood coagulation factor]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Protein-inhibitor complex]]		[[Category: Protein-inhibitor complex]]
	[[Category: Serine proteinase]]		[[Category: Serine proteinase]]

OCA at 15:36, 29 September 2014

OCA — Mon, 29 Sep 2014 15:36:44 GMT

←Older revision		Revision as of 15:36, 29 September 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_1lqd\| PDB=1lqd \| SCENE= }}~~	+	==CRYSTAL STRUCTURE OF FXA IN COMPLEX WITH 45.==
-	===CRYSTAL STRUCTURE OF FXA IN COMPLEX WITH 45.===	+	<StructureSection load='1lqd' size='340' side='right' caption='[[1lqd]], [[Resolution\|resolution]] 2.70Å' scene=''>
-	~~{{ABSTRACT_PUBMED_12061878}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1lqd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LQD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LQD FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CMI:1-(3-CARBAMIMIDOYL-BENZYL)-4-METHYL-1H-INDOLE-2-CARBOXYLIC+ACID+3,5-DIMETHYL-BENZYLAMIDE'>CMI</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1lpg\|1lpg]], [[1lpk\|1lpk]], [[1lpz\|1lpz]], [[1lqe\|1lqe]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Coagulation_factor_Xa Coagulation factor Xa], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.6 3.4.21.6] </span></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lqd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lqd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1lqd RCSB], [http://www.ebi.ac.uk/pdbsum/1lqd PDBsum]</span></td></tr>
		+	<table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/FA10_HUMAN FA10_HUMAN]] Defects in F10 are the cause of factor X deficiency (FA10D) [MIM:[http://omim.org/entry/227600 227600]]. A hemorrhagic disease with variable presentation. Affected individuals can manifest prolonged nasal and mucosal hemorrhage, menorrhagia, hematuria, and occasionally hemarthrosis. Some patients do not have clinical bleeding diathesis.<ref>PMID:2790181</ref> <ref>PMID:1973167</ref> <ref>PMID:1985698</ref> <ref>PMID:7669671</ref> <ref>PMID:8529633</ref> <ref>PMID:7860069</ref> <ref>PMID:8845463</ref> <ref>PMID:8910490</ref> <ref>PMID:10468877</ref> <ref>PMID:10746568</ref> <ref>PMID:10739379</ref> <ref>PMID:11248282</ref> <ref>PMID:11728527</ref> <ref>PMID:12945883</ref> <ref>PMID:15650540</ref> <ref>PMID:17393015</ref> <ref>PMID:19135706</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/FA10_HUMAN FA10_HUMAN]] 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.
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lq/1lqd_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	A series of 138 nonchiral 3-amidinobenzyl-1H-indole-2-carboxamides and analogues as inhibitors of the blood coagulation enzyme factor Xa (fXa) were designed, synthesized, and investigated by X-ray structure analysis and 3D quantitative structure-activity relationship (QSAR) studies (CoMFA, CoMSIA) in order to identify important protein-ligand interactions responsible for biological affinity and selectivity. Several compounds from this series are highly potent and selective inhibitors of this important enzyme linking extrinsic and intrinsic coagulation pathways. To rationalize biological affinity and to provide guidelines for further design, all compounds were docked into the factor Xa binding site. Those docking studies were based on X-ray structures of factor Xa in complex with literature-known inhibitors. It was possible to validate those binding modes by four X-ray crystal structures of representative ligands in factor Xa, while one ligand was additionally crystallized in trypsin to rationalize requirements for selective factor Xa inhibition. The 3D-QSAR models based on a superposition rule derived from these docking studies were validated using conventional and cross-validated r(2) values using the leave-one-out method and repeated analyses using two randomly chosen cross-validation groups plus randomization of biological activities. This led to consistent and highly predictive 3D-QSAR models with good correlation coefficients for both CoMFA and CoMSIA, which were found to correspond to experimentally determined factor Xa binding site topology in terms of steric, electrostatic, and hydrophobic complementarity. Subsets selected as smaller training sets using 2D fingerprints and maximum dissimilarity methods resulted in 3D-QSAR models with remarkable correlation coefficients and a high predictive power. The final quantitative SAR information agrees with all experimental data for the binding topology and thus provides reasonable activity predictions for novel factor Xa inhibitors.

-	~~==Disease==~~	+	Design and quantitative structure-activity relationship of 3-amidinobenzyl-1H-indole-2-carboxamides as potent, nonchiral, and selective inhibitors of blood coagulation factor Xa.,Matter H, Defossa E, Heinelt U, Blohm PM, Schneider D, Muller A, Herok S, Schreuder H, Liesum A, Brachvogel V, Lonze P, Walser A, Al-Obeidi F, Wildgoose P J Med Chem. 2002 Jun 20;45(13):2749-69. PMID:12061878<ref>PMID:12061878</ref>
-	~~[[http://www.uniprot.org/uniprot/FA10_HUMAN FA10_HUMAN]] Defects in F10 are the cause~~ of factor ~~X deficiency (FA10D) [MIM:[http://omim.org/entry/227600 227600]]~~. A ~~hemorrhagic disease with variable presentation. Affected individuals can manifest prolonged nasal and mucosal hemorrhage~~, ~~menorrhagia~~, ~~hematuria~~, ~~and occasionally hemarthrosis~~. ~~Some patients do not have clinical bleeding diathesis~~.~~<ref>~~PMID:2790181</ref><ref>PMID:1973167</ref><ref>PMID:1985698</ref><ref>PMID:7669671</ref><ref>PMID:8529633</ref><ref>PMID:7860069</ref><ref>PMID:8845463</ref><ref>PMID:8910490</ref><ref>PMID:10468877</ref><ref>PMID:10746568</ref><ref>PMID:10739379</ref><ref>PMID:11248282</ref><ref>PMID:11728527</ref><ref>PMID:12945883</ref><ref>PMID:15650540</ref><ref>PMID:17393015</ref><ref>PMID:~~19135706~~</ref>	+

-	~~==Function==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[http:~~/~~/www~~.~~uniprot~~.~~org/uniprot/FA10_HUMAN FA10_HUMAN]] 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~~.	+	</div>
-		+
-	~~==About this Structure==~~	+
-	~~[[1lqd]] is a 2 chain structure with sequence from [http:~~/~~/en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LQD OCA].~~	+

	==See Also==		==See Also==
	*[[Factor Xa\|Factor Xa]]		*[[Factor Xa\|Factor Xa]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:012061878</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Coagulation factor Xa]]		[[Category: Coagulation factor Xa]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

OCA at 17:36, 24 March 2013

OCA — Sun, 24 Mar 2013 17:36:55 GMT

←Older revision		Revision as of 17:36, 24 March 2013
Line 1:		Line 1:
-	[[Image:1lqd.png\|left\|200px]]
-
	{{STRUCTURE_1lqd\| PDB=1lqd \| SCENE= }}		{{STRUCTURE_1lqd\| PDB=1lqd \| SCENE= }}
-
	===CRYSTAL STRUCTURE OF FXA IN COMPLEX WITH 45.===		===CRYSTAL STRUCTURE OF FXA IN COMPLEX WITH 45.===
		+	{{ABSTRACT_PUBMED_12061878}}

-	~~{{ABSTRACT_PUBMED_12061878}}~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/FA10_HUMAN FA10_HUMAN]] Defects in F10 are the cause of factor X deficiency (FA10D) [MIM:[http://omim.org/entry/227600 227600]]. A hemorrhagic disease with variable presentation. Affected individuals can manifest prolonged nasal and mucosal hemorrhage, menorrhagia, hematuria, and occasionally hemarthrosis. Some patients do not have clinical bleeding diathesis.<ref>PMID:2790181</ref><ref>PMID:1973167</ref><ref>PMID:1985698</ref><ref>PMID:7669671</ref><ref>PMID:8529633</ref><ref>PMID:7860069</ref><ref>PMID:8845463</ref><ref>PMID:8910490</ref><ref>PMID:10468877</ref><ref>PMID:10746568</ref><ref>PMID:10739379</ref><ref>PMID:11248282</ref><ref>PMID:11728527</ref><ref>PMID:12945883</ref><ref>PMID:15650540</ref><ref>PMID:17393015</ref><ref>PMID:19135706</ref>
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/FA10_HUMAN FA10_HUMAN]] 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.

	==About this Structure==		==About this Structure==
Line 14:		Line 16:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:012061878</ref><references group="xtra"/>	+	<ref group="xtra">PMID:012061878</ref><references group="xtra"/><references/>
	[[Category: Coagulation factor Xa]]		[[Category: Coagulation factor Xa]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

OCA at 06:12, 20 October 2012

OCA — Sat, 20 Oct 2012 06:12:54 GMT

←Older revision		Revision as of 06:12, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1lqd]] is a 2 chain structure ~~of [[Factor Xa]]~~ with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LQD OCA].	+	[[1lqd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LQD OCA].

	==See Also==		==See Also==

←Older revision		Revision as of 06:48, 18 August 2021
Line 3:		Line 3:
	<StructureSection load='1lqd' size='340' side='right'caption='[[1lqd]], [[Resolution\|resolution]] 2.70Å' scene=''>		<StructureSection load='1lqd' size='340' side='right'caption='[[1lqd]], [[Resolution\|resolution]] 2.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1lqd]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LQD OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1LQD FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1lqd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LQD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LQD FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CMI:1-(3-CARBAMIMIDOYL-BENZYL)-4-METHYL-1H-INDOLE-2-CARBOXYLIC+ACID+3,5-DIMETHYL-BENZYLAMIDE'>CMI</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CMI:1-(3-CARBAMIMIDOYL-BENZYL)-4-METHYL-1H-INDOLE-2-CARBOXYLIC+ACID+3,5-DIMETHYL-BENZYLAMIDE'>CMI</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1lpg\|1lpg]], [[1lpk\|1lpk]], [[1lpz\|1lpz]], [[1lqe\|1lqe]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1lpg\|1lpg]], [[1lpk\|1lpk]], [[1lpz\|1lpz]], [[1lqe\|1lqe]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Coagulation_factor_Xa Coagulation factor Xa], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.6 3.4.21.6] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Coagulation_factor_Xa Coagulation factor Xa], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.6 3.4.21.6] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1lqd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lqd OCA], [~~http~~://pdbe.org/1lqd PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1lqd RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1lqd PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1lqd ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lqd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lqd OCA], [https://pdbe.org/1lqd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lqd RCSB], [https://www.ebi.ac.uk/pdbsum/1lqd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lqd ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/FA10_HUMAN FA10_HUMAN]] Defects in F10 are the cause of factor X deficiency (FA10D) [MIM:[~~http~~://omim.org/entry/227600 227600]]. A hemorrhagic disease with variable presentation. Affected individuals can manifest prolonged nasal and mucosal hemorrhage, menorrhagia, hematuria, and occasionally hemarthrosis. Some patients do not have clinical bleeding diathesis.<ref>PMID:2790181</ref> <ref>PMID:1973167</ref> <ref>PMID:1985698</ref> <ref>PMID:7669671</ref> <ref>PMID:8529633</ref> <ref>PMID:7860069</ref> <ref>PMID:8845463</ref> <ref>PMID:8910490</ref> <ref>PMID:10468877</ref> <ref>PMID:10746568</ref> <ref>PMID:10739379</ref> <ref>PMID:11248282</ref> <ref>PMID:11728527</ref> <ref>PMID:12945883</ref> <ref>PMID:15650540</ref> <ref>PMID:17393015</ref> <ref>PMID:19135706</ref>	+	[[https://www.uniprot.org/uniprot/FA10_HUMAN FA10_HUMAN]] Defects in F10 are the cause of factor X deficiency (FA10D) [MIM:[https://omim.org/entry/227600 227600]]. A hemorrhagic disease with variable presentation. Affected individuals can manifest prolonged nasal and mucosal hemorrhage, menorrhagia, hematuria, and occasionally hemarthrosis. Some patients do not have clinical bleeding diathesis.<ref>PMID:2790181</ref> <ref>PMID:1973167</ref> <ref>PMID:1985698</ref> <ref>PMID:7669671</ref> <ref>PMID:8529633</ref> <ref>PMID:7860069</ref> <ref>PMID:8845463</ref> <ref>PMID:8910490</ref> <ref>PMID:10468877</ref> <ref>PMID:10746568</ref> <ref>PMID:10739379</ref> <ref>PMID:11248282</ref> <ref>PMID:11728527</ref> <ref>PMID:12945883</ref> <ref>PMID:15650540</ref> <ref>PMID:17393015</ref> <ref>PMID:19135706</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/FA10_HUMAN FA10_HUMAN]] 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.	+	[[https://www.uniprot.org/uniprot/FA10_HUMAN FA10_HUMAN]] 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.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]