5n26 - Revision history

OCA at 17:58, 8 November 2023

OCA — Wed, 08 Nov 2023 17:58:13 GMT

←Older revision		Revision as of 17:58, 8 November 2023
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	==X-ray structure of human heavy chain ferritin in complex with cisplatin==		==X-ray structure of human heavy chain ferritin in complex with cisplatin==
-	<StructureSection load='5n26' size='340' side='right' caption='[[5n26]], [[Resolution\|resolution]] 2.05Å' scene=''>	+	<StructureSection load='5n26' size='340' side='right'caption='[[5n26]], [[Resolution\|resolution]] 2.05Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5n26]] is a 1 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=5N26 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5N26 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5n26]] is a 1 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=5N26 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5N26 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=73M:BIS(AZANYL)-CHLORANYL-OXIDANYL-PLATINUM'>73M</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CPT:CISPLATIN'>CPT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.05Å</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FTH1, FTH, FTHL6, OK/SW-cl.84, PIG15 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=73M:BIS(AZANYL)-CHLORANYL-OXIDANYL-PLATINUM'>73M</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CPT:CISPLATIN'>CPT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ferroxidase Ferroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.16.3.1 1.16.3.1] </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=5n26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n26 OCA], [https://pdbe.org/5n26 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5n26 RCSB], [https://www.ebi.ac.uk/pdbsum/5n26 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5n26 ProSAT]</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=5n26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n26 OCA], [~~http~~://pdbe.org/5n26 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5n26 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5n26 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5n26 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/FRIH_HUMAN FRIH_HUMAN]] Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney (By similarity).	+	[https://www.uniprot.org/uniprot/FRIH_HUMAN FRIH_HUMAN] Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney (By similarity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	</div>		</div>
	<div class="pdbe-citations 5n26" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5n26" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Ferritin 3D structures\|Ferritin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Ferroxidase~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~Human~~]]	+	[[Category: Large Structures]]
-	[[Category: Ferraro, G]]	+	[[Category: Ferraro G]]
-	[[Category: Merlino, A]]	+	[[Category: Merlino A]]
-	~~[[Category: Ferritin]]~~	+
-	~~[[Category: Oxidoreductase~~]]	+

OCA at 01:23, 16 November 2017

OCA — Thu, 16 Nov 2017 01:23:01 GMT

←Older revision		Revision as of 01:23, 16 November 2017
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	<StructureSection load='5n26' size='340' side='right' caption='[[5n26]], [[Resolution\|resolution]] 2.05Å' scene=''>		<StructureSection load='5n26' size='340' side='right' caption='[[5n26]], [[Resolution\|resolution]] 2.05Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5n26]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N26 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5N26 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5n26]] is a 1 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=5N26 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5N26 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=73M:BIS(AZANYL)-CHLORANYL-OXIDANYL-PLATINUM'>73M</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CPT:CISPLATIN'>CPT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=73M:BIS(AZANYL)-CHLORANYL-OXIDANYL-PLATINUM'>73M</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CPT:CISPLATIN'>CPT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FTH1, FTH, FTHL6, OK/SW-cl.84, PIG15 ([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/Ferroxidase Ferroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.16.3.1 1.16.3.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ferroxidase Ferroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.16.3.1 1.16.3.1] </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=5n26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n26 OCA], [http://pdbe.org/5n26 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5n26 RCSB], [http://www.ebi.ac.uk/pdbsum/5n26 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5n26 ProSAT]</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=5n26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n26 OCA], [http://pdbe.org/5n26 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5n26 RCSB], [http://www.ebi.ac.uk/pdbsum/5n26 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5n26 ProSAT]</span></td></tr>
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	</StructureSection>		</StructureSection>
	[[Category: Ferroxidase]]		[[Category: Ferroxidase]]
		+	[[Category: Human]]
	[[Category: Ferraro, G]]		[[Category: Ferraro, G]]
	[[Category: Merlino, A]]		[[Category: Merlino, A]]
	[[Category: Ferritin]]		[[Category: Ferritin]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

OCA at 04:06, 4 August 2017

OCA — Fri, 04 Aug 2017 04:06:57 GMT

←Older revision		Revision as of 04:06, 4 August 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5n26 is ~~ON HOLD~~	+	==X-ray structure of human heavy chain ferritin in complex with cisplatin==
		+	<StructureSection load='5n26' size='340' side='right' caption='[[5n26]], [[Resolution\|resolution]] 2.05Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5n26]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N26 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5N26 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=73M:BIS(AZANYL)-CHLORANYL-OXIDANYL-PLATINUM'>73M</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CPT:CISPLATIN'>CPT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ferroxidase Ferroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.16.3.1 1.16.3.1] </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=5n26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n26 OCA], [http://pdbe.org/5n26 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5n26 RCSB], [http://www.ebi.ac.uk/pdbsum/5n26 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5n26 ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/FRIH_HUMAN FRIH_HUMAN]] Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney (By similarity).
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The aim of this work is to identify the cisplatin binding sites on human H-chain ferritin. High-resolution X-ray crystallography reveals that cisplatin binds four distinct protein sites, that is, the side chains of His136 and Lys68, the side chain of His105, the side chain of Cys90 and the side chain of Cys102. These Pt binding sites are compared with those observed for the adduct that cisplatin forms upon encapsulation within horse spleen L-chain ferritin (87% identity with human L-chain ferritin).

-	~~Authors: Ferraro~~, G., ~~Merlino~~, A.	+	Cisplatin Binding Sites in Human H-Chain Ferritin.,Ferraro G, Ciambellotti S, Messori L, Merlino A Inorg Chem. 2017 Jul 24. doi: 10.1021/acs.inorgchem.7b01072. PMID:28737381<ref>PMID:28737381</ref>

-	~~Description: X-ray structure~~ of ~~human heavy chain ferritin in complex with cisplatin~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased Structures~~]]	+	</div>
		+	<div class="pdbe-citations 5n26" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Ferroxidase]]
	[[Category: Ferraro, G]]		[[Category: Ferraro, G]]
	[[Category: Merlino, A]]		[[Category: Merlino, A]]
		+	[[Category: Ferritin]]
		+	[[Category: Oxidoreductase]]

OCA: Protected "5n26" [edit=sysop:move=sysop]

OCA — Thu, 09 Mar 2017 11:56:43 GMT

Protected "5n26" [edit=sysop:move=sysop]

←Older revision

Revision as of 11:56, 9 March 2017

OCA: New page: '''Unreleased structure''' The entry 5n26 is ON HOLD Authors: Ferraro, G., Merlino, A. Description: X-ray structure of human heavy chain ferritin in complex with cisplatin [[Category: ...

OCA — Thu, 09 Mar 2017 11:56:41 GMT

New page: '''Unreleased structure''' The entry 5n26 is ON HOLD Authors: Ferraro, G., Merlino, A. Description: X-ray structure of human heavy chain ferritin in complex with cisplatin [[Category: ...

New page

'''Unreleased structure'''

The entry 5n26 is ON HOLD

Authors: Ferraro, G., Merlino, A.

Description: X-ray structure of human heavy chain ferritin in complex with cisplatin
[[Category: Unreleased Structures]]
[[Category: Ferraro, G]]
[[Category: Merlino, A]]