4k7s - Revision history

OCA at 15:54, 20 September 2023

2023-09-20T15:54:52Z

←Older revision		Revision as of 15:54, 20 September 2023
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4k7s]] is a 3 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=4K7S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4K7S FirstGlance]. <br>		<table><tr><td colspan='2'>[[4k7s]] is a 3 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=4K7S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4K7S FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.76Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=4k7s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k7s OCA], [https://pdbe.org/4k7s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4k7s RCSB], [https://www.ebi.ac.uk/pdbsum/4k7s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4k7s 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=4k7s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k7s OCA], [https://pdbe.org/4k7s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4k7s RCSB], [https://www.ebi.ac.uk/pdbsum/4k7s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4k7s ProSAT]</span></td></tr>
	</table>		</table>

OCA at 11:44, 30 November 2022

2022-11-30T11:44:06Z

←Older revision		Revision as of 11:44, 30 November 2022
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	<StructureSection load='4k7s' size='340' side='right'caption='[[4k7s]], [[Resolution\|resolution]] 1.76Å' scene=''>		<StructureSection load='4k7s' size='340' side='right'caption='[[4k7s]], [[Resolution\|resolution]] 1.76Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4k7s]] is a 3 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=4K7S OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4K7S FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4k7s]] is a 3 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=4K7S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4K7S FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ubq\|1ubq]], [[3n30\|3n30]], [[3n32\|3n32]], [[3ehv\|3ehv]], [[3eec\|3eec]], [[3efu\|3efu]], [[4k7u\|4k7u]], [[4k7w\|4k7w]]</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=4k7s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k7s OCA], [https://pdbe.org/4k7s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4k7s RCSB], [https://www.ebi.ac.uk/pdbsum/4k7s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4k7s ProSAT]</span></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">UBC ([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/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] </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=4k7s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k7s OCA], [~~http~~://pdbe.org/4k7s PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4k7s RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4k7s PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4k7s ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/UBC_HUMAN UBC_HUMAN]] Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.<ref>PMID:16543144</ref> <ref>PMID:19754430</ref>	+	[https://www.uniprot.org/uniprot/UBC_HUMAN UBC_HUMAN] Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.<ref>PMID:16543144</ref> <ref>PMID:19754430</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	==See Also==		==See Also==
-	*[[~~Ubiquitin~~\|~~Ubiquitin~~]]	+	*[[3D structures of ubiquitin\|3D structures of ubiquitin]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Ubiquitin--protein ligase]]~~	+	[[Category: Arnesano F]]
-	[[Category: Arnesano, F]]	+	[[Category: Bottoni A]]
-	[[Category: Bottoni, A]]	+	[[Category: Calvaresi M]]
-	[[Category: Calvaresi, M]]	+	[[Category: Falini G]]
-	[[Category: Falini, G]]	+	[[Category: Fermani S]]
-	[[Category: Fermani, S]]	+	[[Category: Natile G]]
-	[[Category: Natile, G]]	+
-	~~[[Category: Ligase]]~~	+
-	~~[[Category: Zn adduct~~]]	+

OCA at 09:26, 3 April 2019

2019-04-03T09:26:19Z

←Older revision		Revision as of 09:26, 3 April 2019
Line 1:		Line 1:

	==Crystal structure of Zn2-hUb (human ubiquitin) adduct from a solution 35 mM zinc acetate/1.3 mM hUb==		==Crystal structure of Zn2-hUb (human ubiquitin) adduct from a solution 35 mM zinc acetate/1.3 mM hUb==
-	<StructureSection load='4k7s' size='340' side='right' caption='[[4k7s]], [[Resolution\|resolution]] 1.76Å' scene=''>	+	<StructureSection load='4k7s' size='340' side='right'caption='[[4k7s]], [[Resolution\|resolution]] 1.76Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4k7s]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K7S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4K7S FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4k7s]] is a 3 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=4K7S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4K7S FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ubq\|1ubq]], [[3n30\|3n30]], [[3n32\|3n32]], [[3ehv\|3ehv]], [[3eec\|3eec]], [[3efu\|3efu]], [[4k7u\|4k7u]], [[4k7w\|4k7w]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ubq\|1ubq]], [[3n30\|3n30]], [[3n32\|3n32]], [[3ehv\|3ehv]], [[3eec\|3eec]], [[3efu\|3efu]], [[4k7u\|4k7u]], [[4k7w\|4k7w]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">UBC ([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/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] </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=4k7s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k7s OCA], [http://pdbe.org/4k7s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4k7s RCSB], [http://www.ebi.ac.uk/pdbsum/4k7s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4k7s 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=4k7s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k7s OCA], [http://pdbe.org/4k7s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4k7s RCSB], [http://www.ebi.ac.uk/pdbsum/4k7s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4k7s ProSAT]</span></td></tr>
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Ubiquitin--protein ligase]]		[[Category: Ubiquitin--protein ligase]]
	[[Category: Arnesano, F]]		[[Category: Arnesano, F]]

OCA at 07:56, 9 March 2017

2017-03-09T07:56:09Z

←Older revision		Revision as of 07:56, 9 March 2017
Line 3:		Line 3:
	<StructureSection load='4k7s' size='340' side='right' caption='[[4k7s]], [[Resolution\|resolution]] 1.76Å' scene=''>		<StructureSection load='4k7s' size='340' side='right' caption='[[4k7s]], [[Resolution\|resolution]] 1.76Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4k7s]] is a 3 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=4K7S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4K7S FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4k7s]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K7S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4K7S FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ubq\|1ubq]], [[3n30\|3n30]], [[3n32\|3n32]], [[3ehv\|3ehv]], [[3eec\|3eec]], [[3efu\|3efu]], [[4k7u\|4k7u]], [[4k7w\|4k7w]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ubq\|1ubq]], [[3n30\|3n30]], [[3n32\|3n32]], [[3ehv\|3ehv]], [[3eec\|3eec]], [[3efu\|3efu]], [[4k7u\|4k7u]], [[4k7w\|4k7w]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">UBC ([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/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] </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=4k7s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k7s OCA], [http://pdbe.org/4k7s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4k7s RCSB], [http://www.ebi.ac.uk/pdbsum/4k7s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4k7s 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=4k7s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k7s OCA], [http://pdbe.org/4k7s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4k7s RCSB], [http://www.ebi.ac.uk/pdbsum/4k7s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4k7s ProSAT]</span></td></tr>
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	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
-	~~The metal-binding ability of human ubiquitin (hUb) towards a selection of biologically relevant metal~~ ions and complexes has been probed. Different techniques have been used to obtain crystals suitable for crystallographic analysis. In the first type of experiments, crystals of hUb have been soaked in solutions containing copper(II) acetate and two ~~metallodrugs, Zeise salt~~ (~~K[PtCl(3) (eta(2) -C(2) H(4) )]H(2) O) and cisplatin (cis-[PtCl(2) (NH(3) )(2) ]). The Zeise salt is used in a test for hepatitis, whereas cisplatin is one of~~ the most powerful anticancer drugs in clinical use. The Zeise salt readily reacts with hUb crystals to afford an adduct with three platinum residues per protein molecule, Pt(3) -hUb. In contrast, copper(II) ~~acetate and cisplatin were found~~ to ~~be unreactive for contact times up to one hour and to cause degradation~~ of the ~~hUb crystals for longer times. In the second type of experiments~~, ~~hUb was cocrystallized with a solution of copper(II) or zinc(II) acetate or cisplatin. Zinc(II) acetate gives~~, ~~at low metal-to~~-protein molar ratios (8:1), crystals containing one metal ion per three molecules of protein, Zn-hUb(3) (already reported in previous work), whereas at high metal-to-protein ratios (70:1) gives crystals containing three Zn(II) ions per protein molecule, Zn(3) -hUb. In contrast, once again, copper(II) acetate and cisplatin, even at low metal-to-protein ratios, do not give crystalline material. In the soaking experiment, the Zeise anion leads to simultaneous platination of His68, Met1, and Lys6. Present and previous results of cocrystallization experiments performed with Zn(II) and other Group 12 metal ions allow a comprehensive understanding of the metal-ion binding properties of hUb with His68 as the main anchoring site, followed by Met1 and carboxylic groups of Glu16, Glu18, Glu64, Asp21, and Asp32, to be reached. In the case of platinum, Lys6 can also be a binding site. The ~~amount~~ of ~~bound metal ion, with respect~~ to ~~that of~~ the ~~protein~~, ~~appears~~ to ~~be a relevant parameter influencing crystal packing~~.	+	Zinc ions bridging two ubiquitin molecules (with His68 at the interface) contribute to select a subset of conformers from the noncovalent dimer ensemble, thus restricting quaternary structure dynamics, which hampers apo-protein crystallization. The type of selected conformer is shown to determine the crystal packing, which varies from orthorhombic to cubic symmetry.

-	~~Crystallographic analysis~~ of ~~metal-ion binding to human~~ ubiquitin.,~~Arnesano F, Belviso BD, Caliandro R~~, Falini G, ~~Fermani S~~, Natile G~~, Siliqi D~~ Chemistry. ~~2011 Feb 1~~;17(5):~~1569~~-78. doi: 10.1002/chem.~~201001617~~. Epub, ~~2010 Dec~~ 10. PMID:~~21268159~~<ref>PMID:~~21268159~~</ref>	+	Conformational selection of ubiquitin quaternary structures driven by zinc ions.,Fermani S, Falini G, Calvaresi M, Bottoni A, Calo V, Mangini V, Arnesano F, Natile G Chemistry. 2013 Nov 11;19(46):15480-4. doi: 10.1002/chem.201302229. Epub 2013 Oct, 10. PMID:24123543<ref>PMID:24123543</ref>

	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>
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Human]]
	[[Category: Ubiquitin--protein ligase]]		[[Category: Ubiquitin--protein ligase]]
	[[Category: Arnesano, F]]		[[Category: Arnesano, F]]

OCA at 16:30, 5 August 2016

2016-08-05T16:30:36Z

←Older revision		Revision as of 16:30, 5 August 2016
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		+
	==Crystal structure of Zn2-hUb (human ubiquitin) adduct from a solution 35 mM zinc acetate/1.3 mM hUb==		==Crystal structure of Zn2-hUb (human ubiquitin) adduct from a solution 35 mM zinc acetate/1.3 mM hUb==
	<StructureSection load='4k7s' size='340' side='right' caption='[[4k7s]], [[Resolution\|resolution]] 1.76Å' scene=''>		<StructureSection load='4k7s' size='340' side='right' caption='[[4k7s]], [[Resolution\|resolution]] 1.76Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4k7s]] is a 3 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=4K7S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4K7S FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4k7s]] is a 3 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=4K7S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4K7S FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ubq\|1ubq]], [[3n30\|3n30]], [[3n32\|3n32]], [[3ehv\|3ehv]], [[3eec\|3eec]], [[3efu\|3efu]], [[4k7u\|4k7u]], [[4k7w\|4k7w]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ubq\|1ubq]], [[3n30\|3n30]], [[3n32\|3n32]], [[3ehv\|3ehv]], [[3eec\|3eec]], [[3efu\|3efu]], [[4k7u\|4k7u]], [[4k7w\|4k7w]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">UBC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">UBC ([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/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] </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=4k7s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k7s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4k7s RCSB], [http://www.ebi.ac.uk/pdbsum/4k7s 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=4k7s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k7s OCA], [http://pdbe.org/4k7s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4k7s RCSB], [http://www.ebi.ac.uk/pdbsum/4k7s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4k7s ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	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 4k7s" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 26:		Line 28:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Ubiquitin--protein ligase]]		[[Category: Ubiquitin--protein ligase]]
	[[Category: Arnesano, F]]		[[Category: Arnesano, F]]

OCA at 04:01, 25 December 2014

2014-12-25T04:01:06Z

←Older revision		Revision as of 04:01, 25 December 2014
Line 9:		Line 9:
	<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=4k7s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k7s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4k7s RCSB], [http://www.ebi.ac.uk/pdbsum/4k7s 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=4k7s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k7s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4k7s RCSB], [http://www.ebi.ac.uk/pdbsum/4k7s PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/UBC_HUMAN UBC_HUMAN]] Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.<ref>PMID:16543144</ref> <ref>PMID:19754430</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 14:54, 21 December 2014

2014-12-21T14:54:56Z

←Older revision		Revision as of 14:54, 21 December 2014
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-	~~{{STRUCTURE_4k7s\| PDB=4k7s \| SCENE= }}~~	+	==Crystal structure of Zn2-hUb (human ubiquitin) adduct from a solution 35 mM zinc acetate/1.3 mM hUb==
-	===Crystal structure of Zn2-hUb (human ubiquitin) adduct from a solution 35 mM zinc acetate/1.3 mM hUb===	+	<StructureSection load='4k7s' size='340' side='right' caption='[[4k7s]], [[Resolution\|resolution]] 1.76Å' scene=''>
-	~~{{ABSTRACT_PUBMED_21268159}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4k7s]] is a 3 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=4K7S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4K7S FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ubq\|1ubq]], [[3n30\|3n30]], [[3n32\|3n32]], [[3ehv\|3ehv]], [[3eec\|3eec]], [[3efu\|3efu]], [[4k7u\|4k7u]], [[4k7w\|4k7w]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">UBC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] </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=4k7s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k7s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4k7s RCSB], [http://www.ebi.ac.uk/pdbsum/4k7s PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The metal-binding ability of human ubiquitin (hUb) towards a selection of biologically relevant metal ions and complexes has been probed. Different techniques have been used to obtain crystals suitable for crystallographic analysis. In the first type of experiments, crystals of hUb have been soaked in solutions containing copper(II) acetate and two metallodrugs, Zeise salt (K[PtCl(3) (eta(2) -C(2) H(4) )]H(2) O) and cisplatin (cis-[PtCl(2) (NH(3) )(2) ]). The Zeise salt is used in a test for hepatitis, whereas cisplatin is one of the most powerful anticancer drugs in clinical use. The Zeise salt readily reacts with hUb crystals to afford an adduct with three platinum residues per protein molecule, Pt(3) -hUb. In contrast, copper(II) acetate and cisplatin were found to be unreactive for contact times up to one hour and to cause degradation of the hUb crystals for longer times. In the second type of experiments, hUb was cocrystallized with a solution of copper(II) or zinc(II) acetate or cisplatin. Zinc(II) acetate gives, at low metal-to-protein molar ratios (8:1), crystals containing one metal ion per three molecules of protein, Zn-hUb(3) (already reported in previous work), whereas at high metal-to-protein ratios (70:1) gives crystals containing three Zn(II) ions per protein molecule, Zn(3) -hUb. In contrast, once again, copper(II) acetate and cisplatin, even at low metal-to-protein ratios, do not give crystalline material. In the soaking experiment, the Zeise anion leads to simultaneous platination of His68, Met1, and Lys6. Present and previous results of cocrystallization experiments performed with Zn(II) and other Group 12 metal ions allow a comprehensive understanding of the metal-ion binding properties of hUb with His68 as the main anchoring site, followed by Met1 and carboxylic groups of Glu16, Glu18, Glu64, Asp21, and Asp32, to be reached. In the case of platinum, Lys6 can also be a binding site. The amount of bound metal ion, with respect to that of the protein, appears to be a relevant parameter influencing crystal packing.

-	~~==Function==~~	+	Crystallographic analysis of metal-ion binding to human ubiquitin.,Arnesano F, Belviso BD, Caliandro R, Falini G, Fermani S, Natile G, Siliqi D Chemistry. 2011 Feb 1;17(5):1569-78. doi: 10.1002/chem.201001617. Epub, 2010 Dec 10. PMID:21268159<ref>PMID:21268159</ref>
-	~~[[http://www.uniprot.org/uniprot/UBC_HUMAN UBC_HUMAN]] Ubiquitin exists either covalently attached~~ to ~~another protein, or free (unanchored)~~. ~~When covalently bound~~, ~~it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin)~~, a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, ~~when attached to a target protein~~, ~~have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair~~; ~~Lys-11-linked is involved in ERAD~~ (~~endoplasmic reticulum-associated degradation~~) ~~and in cell~~-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. ~~Linear polymer chains formed via attachment by the initiator Met lead to cell signaling~~. ~~Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed~~. ~~When polyubiquitin is free (unanchored-polyubiquitin)~~, ~~it also has distinct roles, such as in activation of protein kinases, and in signaling~~.~~<ref>~~PMID:~~16543144</ref>~~ <ref>PMID:~~19754430~~</ref>	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[4k7s]] is~~ a ~~3 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=4K7S OCA].~~	+	</div>

-	==~~Reference~~==	+	==See Also==
-	~~<ref group~~=~~"xtra">PMID:021268159</ref><ref group~~=~~"xtra">PMID:019030552</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	*[[Ubiquitin\|Ubiquitin]]
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Ubiquitin--protein ligase]]		[[Category: Ubiquitin--protein ligase]]
-	[[Category: Arnesano, F.]]	+	[[Category: Arnesano, F]]
-	[[Category: Bottoni, A.]]	+	[[Category: Bottoni, A]]
-	[[Category: Calvaresi, M.]]	+	[[Category: Calvaresi, M]]
-	[[Category: Falini, G.]]	+	[[Category: Falini, G]]
-	[[Category: Fermani, S.]]	+	[[Category: Fermani, S]]
-	[[Category: Natile, G.]]	+	[[Category: Natile, G]]
	[[Category: Ligase]]		[[Category: Ligase]]
	[[Category: Zn adduct]]		[[Category: Zn adduct]]

OCA at 07:58, 8 May 2013

2013-05-08T07:58:33Z

←Older revision		Revision as of 07:58, 8 May 2013
Line 1:		Line 1:
-	~~'''Unreleased~~ structure~~'''~~	+	{{STRUCTURE_4k7s\| PDB=4k7s \| SCENE= }}
		+	===Crystal structure of Zn2-hUb (human ubiquitin) adduct from a solution 35 mM zinc acetate/1.3 mM hUb===
		+	{{ABSTRACT_PUBMED_21268159}}

-	~~The entry 4k7s~~ is ~~ON HOLD~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/UBC_HUMAN UBC_HUMAN]] Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.<ref>PMID:16543144</ref> <ref>PMID:19754430</ref>

-	~~Authors~~: ~~Fermani, S~~.~~, Falini, G~~.~~, Calvaresi, M~~.~~, Bottoni, A~~.~~, Arnesano, F~~.~~, Natile, G~~.	+	==About this Structure==
		+	[[4k7s]] is a 3 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=4K7S OCA].

-	~~Description~~: ~~Crystal structure of Zn2-hUb (human ubiquitin) adduct from a solution 35 mM zinc acetate~~/1.~~3 mM hUb~~	+	==Reference==
		+	<ref group="xtra">PMID:021268159</ref><ref group="xtra">PMID:019030552</ref><references group="xtra"/><references/>
		+	[[Category: Homo sapiens]]
		+	[[Category: Ubiquitin--protein ligase]]
		+	[[Category: Arnesano, F.]]
		+	[[Category: Bottoni, A.]]
		+	[[Category: Calvaresi, M.]]
		+	[[Category: Falini, G.]]
		+	[[Category: Fermani, S.]]
		+	[[Category: Natile, G.]]
		+	[[Category: Ligase]]
		+	[[Category: Zn adduct]]

OCA: Protected "4k7s" [edit=sysop:move=sysop]

2013-04-24T11:02:12Z

Protected "4k7s" [edit=sysop:move=sysop]

←Older revision

Revision as of 11:02, 24 April 2013

OCA: New page: '''Unreleased structure''' The entry 4k7s is ON HOLD Authors: Fermani, S., Falini, G., Calvaresi, M., Bottoni, A., Arnesano, F., Natile, G. Description: Crystal structure of Zn2-hUb (h...

2013-04-24T11:02:11Z

New page: '''Unreleased structure''' The entry 4k7s is ON HOLD Authors: Fermani, S., Falini, G., Calvaresi, M., Bottoni, A., Arnesano, F., Natile, G. Description: Crystal structure of Zn2-hUb (h...

New page

'''Unreleased structure'''

The entry 4k7s is ON HOLD

Authors: Fermani, S., Falini, G., Calvaresi, M., Bottoni, A., Arnesano, F., Natile, G.

Description: Crystal structure of Zn2-hUb (human ubiquitin) adduct from a solution 35 mM zinc acetate/1.3 mM hUb