3w44 - Revision history

OCA at 05:22, 3 August 2022

2022-08-03T05:22:03Z

←Older revision		Revision as of 05:22, 3 August 2022
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	==Crystal structure of RsbX, selenomethionine derivative==		==Crystal structure of RsbX, selenomethionine derivative==
-	<StructureSection load='3w44' size='340' side='right' caption='[[3w44]], [[Resolution\|resolution]] 2.30Å' scene=''>	+	<StructureSection load='3w44' size='340' side='right'caption='[[3w44]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3w44]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Bacsu Bacsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W44 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3W44 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3w44]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacsu Bacsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W44 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3W44 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3w40\|3w40]], [[3w41\|3w41]], [[3w42\|3w42]], [[3w43\|3w43]], [[3w45\|3w45]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3w40\|3w40]], [[3w41\|3w41]], [[3w42\|3w42]], [[3w43\|3w43]], [[3w45\|3w45]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BSU04740, rsbX ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BSU04740, rsbX ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Phosphoserine_phosphatase Phosphoserine phosphatase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.3 3.1.3.3] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phosphoserine_phosphatase Phosphoserine phosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.3 3.1.3.3] </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=3w44 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w44 OCA], [~~http~~://pdbe.org/3w44 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3w44 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3w44 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3w44 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=3w44 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w44 OCA], [https://pdbe.org/3w44 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w44 RCSB], [https://www.ebi.ac.uk/pdbsum/3w44 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w44 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/RSBX_BACSU RSBX_BACSU]] Negative regulator of sigma-B activity. Dephosphorylates RsbS. Plays a role both in maintaining low sigma-B activity during growth and in reestablishing prestress sigma-B activity after induction. Could have a negative feedback role by indirectly communicating sigma-B protein levels.<ref>PMID:1592822</ref> <ref>PMID:8468294</ref> <ref>PMID:8824586</ref> <ref>PMID:9658013</ref>	+	[[https://www.uniprot.org/uniprot/RSBX_BACSU RSBX_BACSU]] Negative regulator of sigma-B activity. Dephosphorylates RsbS. Plays a role both in maintaining low sigma-B activity during growth and in reestablishing prestress sigma-B activity after induction. Could have a negative feedback role by indirectly communicating sigma-B protein levels.<ref>PMID:1592822</ref> <ref>PMID:8468294</ref> <ref>PMID:8824586</ref> <ref>PMID:9658013</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 30:		Line 30:
	</StructureSection>		</StructureSection>
	[[Category: Bacsu]]		[[Category: Bacsu]]
		+	[[Category: Large Structures]]
	[[Category: Phosphoserine phosphatase]]		[[Category: Phosphoserine phosphatase]]
	[[Category: Baba, S]]		[[Category: Baba, S]]

OCA at 12:11, 12 April 2017

2017-04-12T12:11:16Z

←Older revision		Revision as of 12:11, 12 April 2017
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		+
	==Crystal structure of RsbX, selenomethionine derivative==		==Crystal structure of RsbX, selenomethionine derivative==
	<StructureSection load='3w44' size='340' side='right' caption='[[3w44]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='3w44' size='340' side='right' caption='[[3w44]], [[Resolution\|resolution]] 2.30Å' scene=''>
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	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BSU04740, rsbX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BSU04740, rsbX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoserine_phosphatase Phosphoserine phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.3 3.1.3.3] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoserine_phosphatase Phosphoserine phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.3 3.1.3.3] </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=3w44 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w44 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3w44 RCSB], [http://www.ebi.ac.uk/pdbsum/3w44 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=3w44 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w44 OCA], [http://pdbe.org/3w44 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3w44 RCSB], [http://www.ebi.ac.uk/pdbsum/3w44 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3w44 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 20:		Line 21:
	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 3w44" style="background-color:#fffaf0;"></div>

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

OCA at 12:11, 1 July 2015

2015-07-01T12:11:18Z

←Older revision		Revision as of 12:11, 1 July 2015
Line 12:		Line 12:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/RSBX_BACSU RSBX_BACSU]] Negative regulator of sigma-B activity. Dephosphorylates RsbS. Plays a role both in maintaining low sigma-B activity during growth and in reestablishing prestress sigma-B activity after induction. Could have a negative feedback role by indirectly communicating sigma-B protein levels.<ref>PMID:1592822</ref> <ref>PMID:8468294</ref> <ref>PMID:8824586</ref> <ref>PMID:9658013</ref>		[[http://www.uniprot.org/uniprot/RSBX_BACSU RSBX_BACSU]] Negative regulator of sigma-B activity. Dephosphorylates RsbS. Plays a role both in maintaining low sigma-B activity during growth and in reestablishing prestress sigma-B activity after induction. Could have a negative feedback role by indirectly communicating sigma-B protein levels.<ref>PMID:1592822</ref> <ref>PMID:8468294</ref> <ref>PMID:8824586</ref> <ref>PMID:9658013</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	In the general stress response of Bacillus subtilis, which is governed by the sigma factor sigma(B), stress signalling is relayed by a cascade of Rsb proteins that regulate sigma(B) activity. RsbX, a PPM II phosphatase, halts the response by dephosphorylating the stressosome composed of RsbR and RsbS. The crystal structure of RsbX reveals a reorganization of the catalytic centre, with the second Mn(2+) ion uniquely coordinated by Gly47 O from the beta4-alpha1 loop instead of a water molecule as in PPM I phosphatases. An extra helical turn of alpha1 tilts the loop towards the metal-binding site, and the beta2-beta3 loop swings outwards to accommodate this tilting. The residues critical for this defining feature of the PPM II phosphatases are highly conserved. Formation of the catalytic centre is metal-specific, as crystallization with Mg(2+) ions resulted in a shift of the beta4-alpha1 loop that led to loss of the second ion. RsbX also lacks the flap subdomain characteristic of PPM I phosphatases. On the basis of a stressosome model, the activity of RsbX towards RsbR-P and RsbS-P may be influenced by the different accessibilities of their phosphorylation sites.
		+
		+	Structure of the RsbX phosphatase involved in the general stress response of Bacillus subtilis.,Teh AH, Makino M, Hoshino T, Baba S, Shimizu N, Yamamoto M, Kumasaka T Acta Crystallogr D Biol Crystallogr. 2015 Jun;71(Pt 6):1392-9. doi:, 10.1107/S1399004715007166. Epub 2015 May 23. PMID:26057679<ref>PMID:26057679</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

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

OCA at 11:05, 25 December 2014

2014-12-25T11:05:49Z

←Older revision		Revision as of 11:05, 25 December 2014
Line 10:		Line 10:
	<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=3w44 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w44 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3w44 RCSB], [http://www.ebi.ac.uk/pdbsum/3w44 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=3w44 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w44 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3w44 RCSB], [http://www.ebi.ac.uk/pdbsum/3w44 PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/RSBX_BACSU RSBX_BACSU]] Negative regulator of sigma-B activity. Dephosphorylates RsbS. Plays a role both in maintaining low sigma-B activity during growth and in reestablishing prestress sigma-B activity after induction. Could have a negative feedback role by indirectly communicating sigma-B protein levels.<ref>PMID:1592822</ref> <ref>PMID:8468294</ref> <ref>PMID:8824586</ref> <ref>PMID:9658013</ref>

	==See Also==		==See Also==
	*[[Phosphoserine phosphatase\|Phosphoserine phosphatase]]		*[[Phosphoserine phosphatase\|Phosphoserine phosphatase]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 18:54, 21 December 2014

2014-12-21T18:54:31Z

←Older revision		Revision as of 18:54, 21 December 2014
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-	~~{{STRUCTURE_3w44\| PDB~~=3w44 \| ~~SCENE~~= }}	+	==Crystal structure of RsbX, selenomethionine derivative==
-	===~~Crystal~~ structure ~~of RsbX~~, ~~selenomethionine derivative~~===	+	<StructureSection load='3w44' size='340' side='right' caption='[[3w44]], [[Resolution\|resolution]] 2.30Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3w44]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacsu Bacsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W44 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3W44 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
		+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3w40\|3w40]], [[3w41\|3w41]], [[3w42\|3w42]], [[3w43\|3w43]], [[3w45\|3w45]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BSU04740, rsbX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoserine_phosphatase Phosphoserine phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.3 3.1.3.3] </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=3w44 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w44 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3w44 RCSB], [http://www.ebi.ac.uk/pdbsum/3w44 PDBsum]</span></td></tr>
		+	</table>

-	==~~Function~~==	+	==See Also==
-	[[~~http://www.uniprot.org/uniprot/RSBX_BACSU RSBX_BACSU~~]] Negative regulator of sigma-B activity. Dephosphorylates RsbS. Plays a role both in maintaining low sigma-B activity during growth and in reestablishing prestress sigma-B activity after induction. Could have a negative feedback role by indirectly communicating sigma-B protein levels.<ref>PMID:1592822</~~ref~~> ~~<ref>PMID:8468294</ref> <ref>PMID:8824586</ref> <ref>PMID:9658013</ref>~~	+	*[[Phosphoserine phosphatase\|Phosphoserine phosphatase]]
-		+	__TOC__
-	~~==About this Structure==~~	+	</StructureSection>
-	[[~~3w44~~]] ~~is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W44 OCA].~~	+	[[Category: Bacsu]]
-		+
-	~~==Reference==~~	+
-	~~<references group="xtra"/><references/>~~	+
	[[Category: Phosphoserine phosphatase]]		[[Category: Phosphoserine phosphatase]]
-	[[Category: Baba, S.]]	+	[[Category: Baba, S]]
-	[[Category: Kumasaka, T.]]	+	[[Category: Kumasaka, T]]
-	[[Category: Makino, M.]]	+	[[Category: Makino, M]]
-	[[Category: Shimizu, N.]]	+	[[Category: Shimizu, N]]
-	[[Category: Teh, A H.]]	+	[[Category: Teh, A H]]
-	[[Category: Yamamoto, M.]]	+	[[Category: Yamamoto, M]]
	[[Category: Dephosphorylation]]		[[Category: Dephosphorylation]]
	[[Category: Environmental stress]]		[[Category: Environmental stress]]

OCA at 07:00, 22 January 2014

2014-01-22T07:00:18Z

←Older revision		Revision as of 07:00, 22 January 2014
Line 1:		Line 1:
-	~~'''Unreleased~~ structure~~'''~~	+	{{STRUCTURE_3w44\| PDB=3w44 \| SCENE= }}
		+	===Crystal structure of RsbX, selenomethionine derivative===

-	~~The entry 3w44 is ON HOLD~~ ~~until Paper Publication~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/RSBX_BACSU RSBX_BACSU]] Negative regulator of sigma-B activity. Dephosphorylates RsbS. Plays a role both in maintaining low sigma-B activity during growth and in reestablishing prestress sigma-B activity after induction. Could have a negative feedback role by indirectly communicating sigma-B protein levels.<ref>PMID:1592822</ref> <ref>PMID:8468294</ref> <ref>PMID:8824586</ref> <ref>PMID:9658013</ref>

-	~~Authors~~: ~~Teh, A.H., Makino, M., Baba, S~~.~~, Shimizu, N~~.~~, Yamamoto, M~~.~~, Kumasaka, T~~.	+	==About this Structure==
		+	[[3w44]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W44 OCA].

-	~~Description~~: ~~Crystal structure of RsbX~~, ~~selenomethionine derivative~~	+	==Reference==
		+	<references group="xtra"/><references/>
		+	[[Category: Phosphoserine phosphatase]]
		+	[[Category: Baba, S.]]
		+	[[Category: Kumasaka, T.]]
		+	[[Category: Makino, M.]]
		+	[[Category: Shimizu, N.]]
		+	[[Category: Teh, A H.]]
		+	[[Category: Yamamoto, M.]]
		+	[[Category: Dephosphorylation]]
		+	[[Category: Environmental stress]]
		+	[[Category: Gene expression regulation]]
		+	[[Category: Hydrolase]]
		+	[[Category: Hydrolase protein phosphatase]]
		+	[[Category: Magnesium/manganese binding]]
		+	[[Category: Phosphatase]]
		+	[[Category: Phosphoric monoester hydrolase]]
		+	[[Category: Protein structure]]
		+	[[Category: Signaling protein]]
		+	[[Category: Stressosome]]
		+	[[Category: Tertiary]]

OCA at 14:39, 10 July 2013

2013-07-10T14:39:00Z

←Older revision		Revision as of 14:39, 10 July 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3w44 is ON HOLD	+	The entry 3w44 is ON HOLD until Paper Publication

	Authors: Teh, A.H., Makino, M., Baba, S., Shimizu, N., Yamamoto, M., Kumasaka, T.		Authors: Teh, A.H., Makino, M., Baba, S., Shimizu, N., Yamamoto, M., Kumasaka, T.

	Description: Crystal structure of RsbX, selenomethionine derivative		Description: Crystal structure of RsbX, selenomethionine derivative

OCA: Protected "3w44" [edit=sysop:move=sysop]

2013-01-09T07:37:31Z

Protected "3w44" [edit=sysop:move=sysop]

←Older revision

Revision as of 07:37, 9 January 2013

OCA: New page: '''Unreleased structure''' The entry 3w44 is ON HOLD Authors: Teh, A.H., Makino, M., Baba, S., Shimizu, N., Yamamoto, M., Kumasaka, T. Description: Crystal structure of RsbX, selenomet...

2013-01-09T07:37:29Z

New page: '''Unreleased structure''' The entry 3w44 is ON HOLD Authors: Teh, A.H., Makino, M., Baba, S., Shimizu, N., Yamamoto, M., Kumasaka, T. Description: Crystal structure of RsbX, selenomet...

New page

'''Unreleased structure'''

The entry 3w44 is ON HOLD

Authors: Teh, A.H., Makino, M., Baba, S., Shimizu, N., Yamamoto, M., Kumasaka, T.

Description: Crystal structure of RsbX, selenomethionine derivative