6v64 - Revision history

OCA at 08:04, 11 October 2023

2023-10-11T08:04:18Z

←Older revision		Revision as of 08:04, 11 October 2023
Line 3:		Line 3:
	<StructureSection load='6v64' size='340' side='right'caption='[[6v64]], [[Resolution\|resolution]] 2.29Å' scene=''>		<StructureSection load='6v64' size='340' side='right'caption='[[6v64]], [[Resolution\|resolution]] 2.29Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6v64]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6V64 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=6V64 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6v64]] 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=6V64 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6V64 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0G6:D-PHENYLALANYL-N-[(2S,3S)-6-{[AMINO(IMINIO)METHYL]AMINO}-1-CHLORO-2-HYDROXYHEXAN-3-YL]-L-PROLINAMIDE'>0G6</scene>, <scene name='pdbligand=NA:~~SODIUM+ION~~'>NA</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]] 2.29Å</td></tr>
-	~~<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat">~~<scene name='pdbligand=~~FTR~~:~~FLUOROTRYPTOPHANE~~'>~~FTR~~</scene~~></td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0G6:D-PHENYLALANYL-N-[(2S,3S)-6-{[AMINO(IMINIO)METHYL]AMINO}-1-CHLORO-2-HYDROXYHEXAN-3-YL]-L-PROLINAMIDE'>0G6</scene>, <scene name='pdbligand=FTR:FLUOROTRYPTOPHANE'>FTR</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ppb\|1ppb]]</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=6v64 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6v64 OCA], [https://pdbe.org/6v64 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6v64 RCSB], [https://www.ebi.ac.uk/pdbsum/6v64 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6v64 ProSAT]</span></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">F2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>~~	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thrombin Thrombin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.5 3.4.21.5] </span></td></tr>	+
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=6v64 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6v64 OCA], [~~http~~://pdbe.org/6v64 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6v64 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6v64 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6v64 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/THRB_HUMAN THRB_HUMAN]] Defects in F2 are the cause of factor II deficiency (FA2D) [MIM:[~~http~~://omim.org/entry/613679 613679]]. It is a very rare blood coagulation disorder characterized by mucocutaneous bleeding symptoms. The severity of the bleeding manifestations correlates with blood factor II levels.<ref>PMID:14962227</ref> <ref>PMID:6405779</ref> <ref>PMID:3771562</ref> <ref>PMID:3567158</ref> <ref>PMID:3801671</ref> <ref>PMID:3242619</ref> <ref>PMID:2719946</ref> <ref>PMID:1354985</ref> <ref>PMID:1421398</ref> <ref>PMID:1349838</ref> <ref>PMID:7865694</ref> <ref>PMID:7792730</ref> Genetic variations in F2 may be a cause of susceptibility to ischemic stroke (ISCHSTR) [MIM:[~~http~~://omim.org/entry/601367 601367]]; also known as cerebrovascular accident or cerebral infarction. A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors.<ref>PMID:15534175</ref> Defects in F2 are the cause of thrombophilia due to thrombin defect (THPH1) [MIM:[~~http~~://omim.org/entry/188050 188050]]. It is a multifactorial disorder of hemostasis characterized by abnormal platelet aggregation in response to various agents and recurrent thrombi formation. Note=A common genetic variation in the 3-prime untranslated region of the prothrombin gene is associated with elevated plasma prothrombin levels and an increased risk of venous thrombosis. Defects in F2 are associated with susceptibility to pregnancy loss, recurrent, type 2 (RPRGL2) [MIM:[~~http~~://omim.org/entry/614390 614390]]. A common complication of pregnancy, resulting in spontaneous abortion before the fetus has reached viability. The term includes all miscarriages from the time of conception until 24 weeks of gestation. Recurrent pregnancy loss is defined as 3 or more consecutive spontaneous abortions.<ref>PMID:11506076</ref>	+	[https://www.uniprot.org/uniprot/THRB_HUMAN THRB_HUMAN] Defects in F2 are the cause of factor II deficiency (FA2D) [MIM:[https://omim.org/entry/613679 613679]. It is a very rare blood coagulation disorder characterized by mucocutaneous bleeding symptoms. The severity of the bleeding manifestations correlates with blood factor II levels.<ref>PMID:14962227</ref> <ref>PMID:6405779</ref> <ref>PMID:3771562</ref> <ref>PMID:3567158</ref> <ref>PMID:3801671</ref> <ref>PMID:3242619</ref> <ref>PMID:2719946</ref> <ref>PMID:1354985</ref> <ref>PMID:1421398</ref> <ref>PMID:1349838</ref> <ref>PMID:7865694</ref> <ref>PMID:7792730</ref> Genetic variations in F2 may be a cause of susceptibility to ischemic stroke (ISCHSTR) [MIM:[https://omim.org/entry/601367 601367]; also known as cerebrovascular accident or cerebral infarction. A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors.<ref>PMID:15534175</ref> Defects in F2 are the cause of thrombophilia due to thrombin defect (THPH1) [MIM:[https://omim.org/entry/188050 188050]. It is a multifactorial disorder of hemostasis characterized by abnormal platelet aggregation in response to various agents and recurrent thrombi formation. Note=A common genetic variation in the 3-prime untranslated region of the prothrombin gene is associated with elevated plasma prothrombin levels and an increased risk of venous thrombosis. Defects in F2 are associated with susceptibility to pregnancy loss, recurrent, type 2 (RPRGL2) [MIM:[https://omim.org/entry/614390 614390]. A common complication of pregnancy, resulting in spontaneous abortion before the fetus has reached viability. The term includes all miscarriages from the time of conception until 24 weeks of gestation. Recurrent pregnancy loss is defined as 3 or more consecutive spontaneous abortions.<ref>PMID:11506076</ref>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/THRB_HUMAN THRB_HUMAN]] Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing.<ref>PMID:2856554</ref>	+	[https://www.uniprot.org/uniprot/THRB_HUMAN THRB_HUMAN] Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing.<ref>PMID:2856554</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 24:		Line 21:
	</div>		</div>
	<div class="pdbe-citations 6v64" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 6v64" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Thrombin 3D Structures\|Thrombin 3D Structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Thrombin~~]]	+	[[Category: Chen Z]]
-	[[Category: Cera, E ~~Di]]~~	+	[[Category: Di Cera E]]
-	~~[[Category: Chen, Z~~]]	+	[[Category: Ruben EA]]
-	[[Category: Ruben~~, E A]]~~	+
-	~~[[Category: Hydrolase~~]]	+

OCA at 07:06, 25 June 2020

2020-06-25T07:06:21Z

←Older revision		Revision as of 07:06, 25 June 2020
Line 1:		Line 1:

	==Crystal structure of human thrombin bound to ppack with tryptophans replaced by 5-F-tryptophan==		==Crystal structure of human thrombin bound to ppack with tryptophans replaced by 5-F-tryptophan==
-	<StructureSection load='6v64' size='340' side='right'caption='[[6v64]]' scene=''>	+	<StructureSection load='6v64' size='340' side='right'caption='[[6v64]], [[Resolution\|resolution]] 2.29Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6V64 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6V64 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6v64]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6V64 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6V64 FirstGlance]. <br>
-	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6v64 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6v64 OCA], [http://pdbe.org/6v64 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6v64 RCSB], [http://www.ebi.ac.uk/pdbsum/6v64 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6v64 ProSAT]</span></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0G6:D-PHENYLALANYL-N-[(2S,3S)-6-{[AMINO(IMINIO)METHYL]AMINO}-1-CHLORO-2-HYDROXYHEXAN-3-YL]-L-PROLINAMIDE'>0G6</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
		+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=FTR:FLUOROTRYPTOPHANE'>FTR</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ppb\|1ppb]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">F2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thrombin Thrombin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.5 3.4.21.5] </span></td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6v64 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6v64 OCA], [http://pdbe.org/6v64 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6v64 RCSB], [http://www.ebi.ac.uk/pdbsum/6v64 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6v64 ProSAT]</span></td></tr>
	</table>		</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/THRB_HUMAN THRB_HUMAN]] Defects in F2 are the cause of factor II deficiency (FA2D) [MIM:[http://omim.org/entry/613679 613679]]. It is a very rare blood coagulation disorder characterized by mucocutaneous bleeding symptoms. The severity of the bleeding manifestations correlates with blood factor II levels.<ref>PMID:14962227</ref> <ref>PMID:6405779</ref> <ref>PMID:3771562</ref> <ref>PMID:3567158</ref> <ref>PMID:3801671</ref> <ref>PMID:3242619</ref> <ref>PMID:2719946</ref> <ref>PMID:1354985</ref> <ref>PMID:1421398</ref> <ref>PMID:1349838</ref> <ref>PMID:7865694</ref> <ref>PMID:7792730</ref> Genetic variations in F2 may be a cause of susceptibility to ischemic stroke (ISCHSTR) [MIM:[http://omim.org/entry/601367 601367]]; also known as cerebrovascular accident or cerebral infarction. A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors.<ref>PMID:15534175</ref> Defects in F2 are the cause of thrombophilia due to thrombin defect (THPH1) [MIM:[http://omim.org/entry/188050 188050]]. It is a multifactorial disorder of hemostasis characterized by abnormal platelet aggregation in response to various agents and recurrent thrombi formation. Note=A common genetic variation in the 3-prime untranslated region of the prothrombin gene is associated with elevated plasma prothrombin levels and an increased risk of venous thrombosis. Defects in F2 are associated with susceptibility to pregnancy loss, recurrent, type 2 (RPRGL2) [MIM:[http://omim.org/entry/614390 614390]]. A common complication of pregnancy, resulting in spontaneous abortion before the fetus has reached viability. The term includes all miscarriages from the time of conception until 24 weeks of gestation. Recurrent pregnancy loss is defined as 3 or more consecutive spontaneous abortions.<ref>PMID:11506076</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/THRB_HUMAN THRB_HUMAN]] Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing.<ref>PMID:2856554</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The conformational properties of trypsin-like proteases and their zymogen forms remain controversial because of a lack of sufficient information on their free forms. Specifically, it is unclear whether the free protease is zymogen-like and shifts to its mature form upon a ligand induced fit or exists in multiple conformations in equilibrium from which the ligand selects the optimal fit via conformational selection. Here we report the results of 19F NMR measurements that reveal the conformational properties of a protease and its zymogen precursor in the free form. Using the trypsin-like, clotting protease thrombin as a relevant model system, we show that its conformation is quite different from that of its direct zymogen precursor prethrombin-2 and more similar to that of its fully active Na+-bound form. The results cast doubts on recent hypotheses that free thrombin is zymogen-like and transitions to protease-like forms upon ligand binding. Rather, they validate the scenario emerged from previous findings of X-ray crystallography and rapid kinetics supporting a pre-existing equilibrium between open (E) and closed (E) forms of the active site. In this scenario, prethrombin-2 is more dynamic and exists predominantly in the E form, whereas thrombin is more rigid and exists predominantly in the E form. Ligand binding to thrombin takes place exclusively in the E form without significant changes in the overall conformation. In summary, these results disclose the structural architecture of the fee forms of thrombin and prethrombin-2, consistent with an E*-E equilibrium and providing no evidence that free thrombin is zymogen-like.
		+
		+	19F NMR reveals the conformational properties of free thrombin and its zymogen precursor prethrombin-2.,Ruben EA, Gandhi PS, Chen Z, Koester SK, DeKoster GT, Frieden C, Di Cera E J Biol Chem. 2020 May 1. pii: RA120.013419. doi: 10.1074/jbc.RA120.013419. PMID:32358061<ref>PMID:32358061</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6v64" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Chen Z~~]]	+	[[Category: Thrombin]]
-	[[Category: Di Cera E]]	+	[[Category: Cera, E Di]]
-	[[Category: Ruben EA]]	+	[[Category: Chen, Z]]
		+	[[Category: Ruben, E A]]
		+	[[Category: Hydrolase]]

OCA at 05:34, 13 May 2020

2020-05-13T05:34:07Z

←Older revision		Revision as of 05:34, 13 May 2020
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry 6v64 is ON HOLD until Dec 04 2021~~	+	==Crystal structure of human thrombin bound to ppack with tryptophans replaced by 5-F-tryptophan==
-		+	<StructureSection load='6v64' size='340' side='right'caption='[[6v64]]' scene=''>
-	~~Authors: Ruben, E.A., Chen, Z., Di Cera, E.~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6V64 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6V64 FirstGlance]. <br>
-	~~Description:~~ Crystal structure of human thrombin bound to ppack with tryptophans replaced by 5-F-tryptophan	+	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6v64 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6v64 OCA], [http://pdbe.org/6v64 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6v64 RCSB], [http://www.ebi.ac.uk/pdbsum/6v64 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6v64 ProSAT]</span></td></tr>
-	[[~~Category~~: ~~Unreleased Structures~~]]	+	</table>
-	[[~~Category~~: ~~Di Cera~~, E]]	+	__TOC__
-	[[Category: Chen, Z]]	+	</StructureSection>
-	[[Category: ~~Ruben,~~ E.A]]	+	[[Category: Large Structures]]
		+	[[Category: Chen Z]]
		+	[[Category: Di Cera E]]
		+	[[Category: Ruben EA]]

OCA at 13:30, 29 January 2020

2020-01-29T13:30:22Z

←Older revision		Revision as of 13:30, 29 January 2020
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6v64 is ON HOLD	+	The entry 6v64 is ON HOLD until Dec 04 2021

	Authors: Ruben, E.A., Chen, Z., Di Cera, E.		Authors: Ruben, E.A., Chen, Z., Di Cera, E.
Line 7:		Line 7:
	Description: Crystal structure of human thrombin bound to ppack with tryptophans replaced by 5-F-tryptophan		Description: Crystal structure of human thrombin bound to ppack with tryptophans replaced by 5-F-tryptophan
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: Ruben, E.A]]
	[[Category: Di Cera, E]]		[[Category: Di Cera, E]]
	[[Category: Chen, Z]]		[[Category: Chen, Z]]
		+	[[Category: Ruben, E.A]]

OCA at 06:01, 18 December 2019

2019-12-18T06:01:30Z

←Older revision		Revision as of 06:01, 18 December 2019
Line 5:		Line 5:
	Authors: Ruben, E.A., Chen, Z., Di Cera, E.		Authors: Ruben, E.A., Chen, Z., Di Cera, E.

-	Description: Crystal structure of human thrombin bound to ppack with tryptophans replaced by 5-F-tryptophan.	+	Description: Crystal structure of human thrombin bound to ppack with tryptophans replaced by 5-F-tryptophan
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
		+	[[Category: Ruben, E.A]]
	[[Category: Di Cera, E]]		[[Category: Di Cera, E]]
	[[Category: Chen, Z]]		[[Category: Chen, Z]]
-	[[Category: Ruben, E.A]]

OCA: Protected "6v64" [edit=sysop:move=sysop]

2019-12-11T13:48:28Z

Protected "6v64" [edit=sysop:move=sysop]

←Older revision

Revision as of 13:48, 11 December 2019

OCA: New page: '''Unreleased structure''' The entry 6v64 is ON HOLD Authors: Ruben, E.A., Chen, Z., Di Cera, E. Description: Crystal structure of human thrombin bound to ppack with tryptophans replac...

2019-12-11T13:48:26Z

New page: '''Unreleased structure''' The entry 6v64 is ON HOLD Authors: Ruben, E.A., Chen, Z., Di Cera, E. Description: Crystal structure of human thrombin bound to ppack with tryptophans replac...

New page

'''Unreleased structure'''

The entry 6v64 is ON HOLD

Authors: Ruben, E.A., Chen, Z., Di Cera, E.

Description: Crystal structure of human thrombin bound to ppack with tryptophans replaced by 5-F-tryptophan.
[[Category: Unreleased Structures]]
[[Category: Di Cera, E]]
[[Category: Chen, Z]]
[[Category: Ruben, E.A]]