2n9i - Revision history

OCA at 10:24, 15 March 2023

OCA — Wed, 15 Mar 2023 10:24:40 GMT

←Older revision		Revision as of 10:24, 15 March 2023
Line 1:		Line 1:

	==Solution structure of reduced human cytochrome c==		==Solution structure of reduced human cytochrome c==
-	<StructureSection load='2n9i' size='340' side='right'caption='[[2n9i~~]], [[NMR_Ensembles_of_Models \| 20 NMR models~~]]' scene=''>	+	<StructureSection load='2n9i' size='340' side='right'caption='[[2n9i]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2n9i]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N9I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N9I FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2n9i]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N9I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N9I FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2n9j\|2n9j]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CYCS, CYC ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2n9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n9i OCA], [https://pdbe.org/2n9i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n9i RCSB], [https://www.ebi.ac.uk/pdbsum/2n9i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n9i 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=2n9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n9i OCA], [https://pdbe.org/2n9i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n9i RCSB], [https://www.ebi.ac.uk/pdbsum/2n9i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n9i ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/CYC_HUMAN CYC_HUMAN]] Defects in CYCS are the cause of thrombocytopenia type 4 (THC4) [MIM:[https://omim.org/entry/612004 612004]]; also known as autosomal dominant thrombocytopenia type 4. Thrombocytopenia is the presence of relatively few platelets in blood. THC4 is a non-syndromic form of thrombocytopenia. Clinical manifestations of thrombocytopenia are absent or mild. THC4 may be caused by dysregulated platelet formation.<ref>PMID:18345000</ref>	+	[https://www.uniprot.org/uniprot/CYC_HUMAN CYC_HUMAN] Defects in CYCS are the cause of thrombocytopenia type 4 (THC4) [MIM:[https://omim.org/entry/612004 612004]; also known as autosomal dominant thrombocytopenia type 4. Thrombocytopenia is the presence of relatively few platelets in blood. THC4 is a non-syndromic form of thrombocytopenia. Clinical manifestations of thrombocytopenia are absent or mild. THC4 may be caused by dysregulated platelet formation.<ref>PMID:18345000</ref>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/CYC_HUMAN CYC_HUMAN]] Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain. Plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol. Binding of cytochrome c to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases.	+	[https://www.uniprot.org/uniprot/CYC_HUMAN CYC_HUMAN] Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain. Plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol. Binding of cytochrome c to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 26:		Line 24:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Imai, M]]	+	[[Category: Imai M]]
-	[[Category: Inagaki, F]]	+	[[Category: Inagaki F]]
-	[[Category: Ishimori, K]]	+	[[Category: Ishimori K]]
-	[[Category: Kumeta, H]]	+	[[Category: Kumeta H]]
-	[[Category: Saio, T]]	+	[[Category: Saio T]]
-	[[Category: Uchida, T]]	+	[[Category: Uchida T]]
-	~~[[Category: Cytochrome c]]~~	+
-	~~[[Category: Electron transfer]]~~	+
-	~~[[Category: Electron transport~~]]	+

OCA at 15:42, 8 June 2021

OCA — Tue, 08 Jun 2021 15:42:41 GMT

←Older revision		Revision as of 15:42, 8 June 2021
Line 1:		Line 1:

	==Solution structure of reduced human cytochrome c==		==Solution structure of reduced human cytochrome c==
-	<StructureSection load='2n9i' size='340' side='right' caption='[[2n9i]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>	+	<StructureSection load='2n9i' size='340' side='right'caption='[[2n9i]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2n9i]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N9I OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2N9I FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2n9i]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N9I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N9I FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2n9j\|2n9j]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2n9j\|2n9j]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CYCS, CYC ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CYCS, CYC ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2n9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n9i OCA], [~~http~~://pdbe.org/2n9i PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2n9i RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2n9i PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2n9i 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=2n9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n9i OCA], [https://pdbe.org/2n9i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n9i RCSB], [https://www.ebi.ac.uk/pdbsum/2n9i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n9i ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/CYC_HUMAN CYC_HUMAN]] Defects in CYCS are the cause of thrombocytopenia type 4 (THC4) [MIM:[~~http~~://omim.org/entry/612004 612004]]; also known as autosomal dominant thrombocytopenia type 4. Thrombocytopenia is the presence of relatively few platelets in blood. THC4 is a non-syndromic form of thrombocytopenia. Clinical manifestations of thrombocytopenia are absent or mild. THC4 may be caused by dysregulated platelet formation.<ref>PMID:18345000</ref>	+	[[https://www.uniprot.org/uniprot/CYC_HUMAN CYC_HUMAN]] Defects in CYCS are the cause of thrombocytopenia type 4 (THC4) [MIM:[https://omim.org/entry/612004 612004]]; also known as autosomal dominant thrombocytopenia type 4. Thrombocytopenia is the presence of relatively few platelets in blood. THC4 is a non-syndromic form of thrombocytopenia. Clinical manifestations of thrombocytopenia are absent or mild. THC4 may be caused by dysregulated platelet formation.<ref>PMID:18345000</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/CYC_HUMAN CYC_HUMAN]] Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain. Plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol. Binding of cytochrome c to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases.	+	[[https://www.uniprot.org/uniprot/CYC_HUMAN CYC_HUMAN]] Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain. Plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol. Binding of cytochrome c to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 27:		Line 27:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Imai, M]]		[[Category: Imai, M]]
	[[Category: Inagaki, F]]		[[Category: Inagaki, F]]

OCA at 17:13, 15 August 2018

OCA — Wed, 15 Aug 2018 17:13:07 GMT

←Older revision		Revision as of 17:13, 15 August 2018
Line 3:		Line 3:
	<StructureSection load='2n9i' size='340' side='right' caption='[[2n9i]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='2n9i' size='340' side='right' caption='[[2n9i]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2n9i]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N9I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2N9I FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2n9i]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N9I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2N9I FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2n9j\|2n9j]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2n9j\|2n9j]]</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=2n9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n9i OCA], [http://pdbe.org/2n9i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2n9i RCSB], [http://www.ebi.ac.uk/pdbsum/2n9i PDBsum]</span></td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CYCS, CYC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2n9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n9i OCA], [http://pdbe.org/2n9i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2n9i RCSB], [http://www.ebi.ac.uk/pdbsum/2n9i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2n9i ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 25:		Line 26:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Imai, M]]		[[Category: Imai, M]]
	[[Category: Inagaki, F]]		[[Category: Inagaki, F]]

OCA at 02:37, 21 February 2016

OCA — Sun, 21 Feb 2016 02:37:59 GMT

←Older revision		Revision as of 02:37, 21 February 2016
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 2n9i is ~~ON HOLD~~	+	==Solution structure of reduced human cytochrome c==
		+	<StructureSection load='2n9i' size='340' side='right' caption='[[2n9i]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2n9i]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N9I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2N9I FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2n9j\|2n9j]]</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=2n9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n9i OCA], [http://pdbe.org/2n9i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2n9i RCSB], [http://www.ebi.ac.uk/pdbsum/2n9i PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/CYC_HUMAN CYC_HUMAN]] Defects in CYCS are the cause of thrombocytopenia type 4 (THC4) [MIM:[http://omim.org/entry/612004 612004]]; also known as autosomal dominant thrombocytopenia type 4. Thrombocytopenia is the presence of relatively few platelets in blood. THC4 is a non-syndromic form of thrombocytopenia. Clinical manifestations of thrombocytopenia are absent or mild. THC4 may be caused by dysregulated platelet formation.<ref>PMID:18345000</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/CYC_HUMAN CYC_HUMAN]] Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain. Plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol. Binding of cytochrome c to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Redox-dependent changes in the structure and dynamics of human cytochrome c (Cyt c) were investigated by solution NMR. We found significant structural changes in several regions, including residues 23-28 (loop 3), which were further corroborated by chemical shift differences between the reduced and oxidized states of Cyt c. These differences are essential for discriminating redox states in Cyt c by cytochrome c oxidase (CcO) during electron transfer reactions. Carr-Purcell-Meiboom-Gill (CPMG) relaxation dispersion experiments identified that the region around His33 undergoes conformational exchanges on the mus-ms timescale, indicating significant redox-dependent structural changes. Because His33 is not part of the interaction site for CcO, our data suggest that the dynamic properties of the region, which is far from the interaction site for CcO, contribute to conformational changes during electron transfer to CcO.

-	~~Authors: Imai~~, M., Saio, T., Kumeta, H., Uchida, T., Inagaki, F., Ishimori, K.	+	Investigation of the redox-dependent modulation of structure and dynamics in human cytochrome c.,Imai M, Saio T, Kumeta H, Uchida T, Inagaki F, Ishimori K Biochem Biophys Res Commun. 2016 Jan 22;469(4):978-84. doi:, 10.1016/j.bbrc.2015.12.079. Epub 2015 Dec 22. PMID:26718409<ref>PMID:26718409</ref>

-	~~Description: Solution structure~~ of ~~reduced human cytochrome c~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[Category~~: ~~Unreleased Structures]]~~	+	</div>
-	~~[[Category: Ishimori, K]]~~	+	<div class="pdbe-citations 2n9i" style="background-color:#fffaf0;"></div>
-	[[Category: ~~Uchida~~, T]]	+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Imai, M]]
	[[Category: Inagaki, F]]		[[Category: Inagaki, F]]
		+	[[Category: Ishimori, K]]
	[[Category: Kumeta, H]]		[[Category: Kumeta, H]]
	[[Category: Saio, T]]		[[Category: Saio, T]]
-	[[Category: ~~Imai~~, M]]	+	[[Category: Uchida, T]]
		+	[[Category: Cytochrome c]]
		+	[[Category: Electron transfer]]
		+	[[Category: Electron transport]]

OCA: Protected "2n9i" [edit=sysop:move=sysop]

OCA — Wed, 02 Dec 2015 10:30:01 GMT

Protected "2n9i" [edit=sysop:move=sysop]

←Older revision

Revision as of 10:30, 2 December 2015

OCA: New page: '''Unreleased structure''' The entry 2n9i is ON HOLD Authors: Imai, M., Saio, T., Kumeta, H., Uchida, T., Inagaki, F., Ishimori, K. Description: Solution structure of reduced human cyt...

OCA — Wed, 02 Dec 2015 10:29:59 GMT

New page: '''Unreleased structure''' The entry 2n9i is ON HOLD Authors: Imai, M., Saio, T., Kumeta, H., Uchida, T., Inagaki, F., Ishimori, K. Description: Solution structure of reduced human cyt...

New page

'''Unreleased structure'''

The entry 2n9i is ON HOLD

Authors: Imai, M., Saio, T., Kumeta, H., Uchida, T., Inagaki, F., Ishimori, K.

Description: Solution structure of reduced human cytochrome c
[[Category: Unreleased Structures]]
[[Category: Ishimori, K]]
[[Category: Uchida, T]]
[[Category: Inagaki, F]]
[[Category: Kumeta, H]]
[[Category: Saio, T]]
[[Category: Imai, M]]