5jpc - Revision history

OCA at 12:38, 6 March 2024

2024-03-06T12:38:00Z

←Older revision		Revision as of 12:38, 6 March 2024
Line 10:		Line 10:
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/MQMTN_HELPJ MQMTN_HELPJ] Catalyzes the direct conversion of aminodeoxyfutalosine (AFL) into dehypoxanthine futalosine (DHFL) and adenine via the hydrolysis of the N-glycosidic bond; this reaction seems to represent an essential step in the menaquinone biosynthesis pathway in Helicobacter species. Also catalyzes the hydrolysis of 5'-methylthioadenosine (MTA) to adenine and 5'-methylthioribose. Can also probably use S-adenosylhomocysteine (SAH) as substrate, leading to adenine and S-ribosylhomocysteine. These other activities highlight the tremendous versatility of the enzyme, which also plays key roles in S-adenosylmethionine recycling and in the biosynthesis of the quorum-sensing molecule autoinducer-2.<ref>PMID:20954236</ref> <ref>PMID:22891633</ref>		[https://www.uniprot.org/uniprot/MQMTN_HELPJ MQMTN_HELPJ] Catalyzes the direct conversion of aminodeoxyfutalosine (AFL) into dehypoxanthine futalosine (DHFL) and adenine via the hydrolysis of the N-glycosidic bond; this reaction seems to represent an essential step in the menaquinone biosynthesis pathway in Helicobacter species. Also catalyzes the hydrolysis of 5'-methylthioadenosine (MTA) to adenine and 5'-methylthioribose. Can also probably use S-adenosylhomocysteine (SAH) as substrate, leading to adenine and S-ribosylhomocysteine. These other activities highlight the tremendous versatility of the enzyme, which also plays key roles in S-adenosylmethionine recycling and in the biosynthesis of the quorum-sensing molecule autoinducer-2.<ref>PMID:20954236</ref> <ref>PMID:22891633</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	MTAN (5'-methylthioadenosine nucleosidase) catalyzes the hydrolysis of the N-ribosidic bond of a variety of adenosine-containing metabolites. The Helicobacter pylori MTAN (HpMTAN) hydrolyzes 6-amino-6-deoxyfutalosine in the second step of the alternative menaquinone biosynthetic pathway. Substrate binding of the adenine moiety is mediated almost exclusively by hydrogen bonds, and the proposed catalytic mechanism requires multiple proton-transfer events. Of particular interest is the protonation state of residue D198, which possesses a pKa above 8 and functions as a general acid to initiate the enzymatic reaction. In this study we present three corefined neutron/X-ray crystal structures of wild-type HpMTAN cocrystallized with S-adenosylhomocysteine (SAH), Formycin A (FMA), and (3R,4S)-4-(4-Chlorophenylthiomethyl)-1-[(9-deaza-adenin-9-yl)methyl]-3-hydroxypyr rolidine (p-ClPh-Thio-DADMe-ImmA) as well as one neutron/X-ray crystal structure of an inactive variant (HpMTAN-D198N) cocrystallized with SAH. These results support a mechanism of D198 pKa elevation through the unexpected sharing of a proton with atom N7 of the adenine moiety possessing unconventional hydrogen-bond geometry. Additionally, the neutron structures also highlight active site features that promote the stabilization of the transition state and slight variations in these interactions that result in 100-fold difference in binding affinities between the DADMe-ImmA and ImmA analogs.
-
-	Neutron structures of the Helicobacter pylori 5'-methylthioadenosine nucleosidase highlight proton sharing and protonation states.,Banco MT, Mishra V, Ostermann A, Schrader TE, Evans GB, Kovalevsky A, Ronning DR Proc Natl Acad Sci U S A. 2016 Nov 29;113(48):13756-13761. Epub 2016 Nov 16. PMID:27856757<ref>PMID:27856757</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 5jpc" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 19:01, 20 September 2023

2023-09-20T19:01:38Z

←Older revision		Revision as of 19:01, 20 September 2023
Line 3:		Line 3:
	<StructureSection load='5jpc' size='340' side='right'caption='[[5jpc]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='5jpc' size='340' side='right'caption='[[5jpc]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5jpc]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Atcc_43504 Atcc 43504~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JPC OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5JPC FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5jpc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JPC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JPC FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</scene>, <scene name='pdbligand=FMC:(1S)-1-(7-AMINO-1H-PYRAZOLO[4,3-D]PYRIMIDIN-3-YL)-1,4-ANHYDRO-D-RIBITOL'>FMC</scene>~~</td></tr>~~	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Hybrid , Neutron Diffraction , X-ray diffraction, [[Resolution\|Resolution]] 2.5Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5k1z\|5k1z]]</td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</scene>, <scene name='pdbligand=FMC:(1S)-1-(7-AMINO-1H-PYRAZOLO[4,3-D]PYRIMIDIN-3-YL)-1,4-ANHYDRO-D-RIBITOL'>FMC</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">mtnN, mtn, jhp_0082 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210 ATCC 43504])</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=5jpc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jpc OCA], [https://pdbe.org/5jpc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jpc RCSB], [https://www.ebi.ac.uk/pdbsum/5jpc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jpc ProSAT]</span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=5jpc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jpc OCA], [~~http~~://pdbe.org/5jpc PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5jpc RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5jpc PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5jpc ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/MQMTN_HELPJ MQMTN_HELPJ]] Catalyzes the direct conversion of aminodeoxyfutalosine (AFL) into dehypoxanthine futalosine (DHFL) and adenine via the hydrolysis of the N-glycosidic bond; this reaction seems to represent an essential step in the menaquinone biosynthesis pathway in Helicobacter species. Also catalyzes the hydrolysis of 5'-methylthioadenosine (MTA) to adenine and 5'-methylthioribose. Can also probably use S-adenosylhomocysteine (SAH) as substrate, leading to adenine and S-ribosylhomocysteine. These other activities highlight the tremendous versatility of the enzyme, which also plays key roles in S-adenosylmethionine recycling and in the biosynthesis of the quorum-sensing molecule autoinducer-2.<ref>PMID:20954236</ref> <ref>PMID:22891633</ref>	+	[https://www.uniprot.org/uniprot/MQMTN_HELPJ MQMTN_HELPJ] Catalyzes the direct conversion of aminodeoxyfutalosine (AFL) into dehypoxanthine futalosine (DHFL) and adenine via the hydrolysis of the N-glycosidic bond; this reaction seems to represent an essential step in the menaquinone biosynthesis pathway in Helicobacter species. Also catalyzes the hydrolysis of 5'-methylthioadenosine (MTA) to adenine and 5'-methylthioribose. Can also probably use S-adenosylhomocysteine (SAH) as substrate, leading to adenine and S-ribosylhomocysteine. These other activities highlight the tremendous versatility of the enzyme, which also plays key roles in S-adenosylmethionine recycling and in the biosynthesis of the quorum-sensing molecule autoinducer-2.<ref>PMID:20954236</ref> <ref>PMID:22891633</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 24:		Line 23:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Atcc 43504]]
-	[[Category: Large Structures]]
-	[[Category: Banco, M T]]
-	[[Category: Kovalevsky, A Y]]
-	[[Category: Ronning, D R]]
	[[Category: Helicobacter pylori]]		[[Category: Helicobacter pylori]]
-	[[Category: ~~Hydrolase~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Joint neutron and x-ray~~]]	+	[[Category: Banco MT]]
-	[[Category: ~~Neutron~~]]	+	[[Category: Kovalevsky AY]]
-	[[Category: ~~Nucleosidase~~]]	+	[[Category: Ronning DR]]

OCA at 11:32, 17 June 2020

2020-06-17T11:32:57Z

←Older revision		Revision as of 11:32, 17 June 2020
Line 1:		Line 1:

	==Joint X-ray/neutron structure of MTAN complex with Formycin A==		==Joint X-ray/neutron structure of MTAN complex with Formycin A==
-	<StructureSection load='5jpc' size='340' side='right' caption='[[5jpc]], [[Resolution\|resolution]] 2.50Å' scene=''>	+	<StructureSection load='5jpc' size='340' side='right'caption='[[5jpc]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5jpc]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JPC OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5JPC FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5jpc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43504 Atcc 43504]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JPC OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5JPC FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</scene>, <scene name='pdbligand=FMC:(1S)-1-(7-AMINO-1H-PYRAZOLO[4,3-D]PYRIMIDIN-3-YL)-1,4-ANHYDRO-D-RIBITOL'>FMC</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</scene>, <scene name='pdbligand=FMC:(1S)-1-(7-AMINO-1H-PYRAZOLO[4,3-D]PYRIMIDIN-3-YL)-1,4-ANHYDRO-D-RIBITOL'>FMC</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5k1z\|5k1z]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5k1z\|5k1z]]</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=5jpc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jpc OCA], [http://pdbe.org/5jpc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jpc RCSB], [http://www.ebi.ac.uk/pdbsum/5jpc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jpc ProSAT]</span></td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">mtnN, mtn, jhp_0082 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210 ATCC 43504])</td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5jpc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jpc OCA], [http://pdbe.org/5jpc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jpc RCSB], [http://www.ebi.ac.uk/pdbsum/5jpc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jpc ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 23:		Line 24:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Atcc 43504]]
		+	[[Category: Large Structures]]
	[[Category: Banco, M T]]		[[Category: Banco, M T]]
	[[Category: Kovalevsky, A Y]]		[[Category: Kovalevsky, A Y]]

OCA at 14:45, 22 December 2016

2016-12-22T14:45:12Z

←Older revision		Revision as of 14:45, 22 December 2016
Line 10:		Line 10:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/MQMTN_HELPJ MQMTN_HELPJ]] Catalyzes the direct conversion of aminodeoxyfutalosine (AFL) into dehypoxanthine futalosine (DHFL) and adenine via the hydrolysis of the N-glycosidic bond; this reaction seems to represent an essential step in the menaquinone biosynthesis pathway in Helicobacter species. Also catalyzes the hydrolysis of 5'-methylthioadenosine (MTA) to adenine and 5'-methylthioribose. Can also probably use S-adenosylhomocysteine (SAH) as substrate, leading to adenine and S-ribosylhomocysteine. These other activities highlight the tremendous versatility of the enzyme, which also plays key roles in S-adenosylmethionine recycling and in the biosynthesis of the quorum-sensing molecule autoinducer-2.<ref>PMID:20954236</ref> <ref>PMID:22891633</ref>		[[http://www.uniprot.org/uniprot/MQMTN_HELPJ MQMTN_HELPJ]] Catalyzes the direct conversion of aminodeoxyfutalosine (AFL) into dehypoxanthine futalosine (DHFL) and adenine via the hydrolysis of the N-glycosidic bond; this reaction seems to represent an essential step in the menaquinone biosynthesis pathway in Helicobacter species. Also catalyzes the hydrolysis of 5'-methylthioadenosine (MTA) to adenine and 5'-methylthioribose. Can also probably use S-adenosylhomocysteine (SAH) as substrate, leading to adenine and S-ribosylhomocysteine. These other activities highlight the tremendous versatility of the enzyme, which also plays key roles in S-adenosylmethionine recycling and in the biosynthesis of the quorum-sensing molecule autoinducer-2.<ref>PMID:20954236</ref> <ref>PMID:22891633</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	MTAN (5'-methylthioadenosine nucleosidase) catalyzes the hydrolysis of the N-ribosidic bond of a variety of adenosine-containing metabolites. The Helicobacter pylori MTAN (HpMTAN) hydrolyzes 6-amino-6-deoxyfutalosine in the second step of the alternative menaquinone biosynthetic pathway. Substrate binding of the adenine moiety is mediated almost exclusively by hydrogen bonds, and the proposed catalytic mechanism requires multiple proton-transfer events. Of particular interest is the protonation state of residue D198, which possesses a pKa above 8 and functions as a general acid to initiate the enzymatic reaction. In this study we present three corefined neutron/X-ray crystal structures of wild-type HpMTAN cocrystallized with S-adenosylhomocysteine (SAH), Formycin A (FMA), and (3R,4S)-4-(4-Chlorophenylthiomethyl)-1-[(9-deaza-adenin-9-yl)methyl]-3-hydroxypyr rolidine (p-ClPh-Thio-DADMe-ImmA) as well as one neutron/X-ray crystal structure of an inactive variant (HpMTAN-D198N) cocrystallized with SAH. These results support a mechanism of D198 pKa elevation through the unexpected sharing of a proton with atom N7 of the adenine moiety possessing unconventional hydrogen-bond geometry. Additionally, the neutron structures also highlight active site features that promote the stabilization of the transition state and slight variations in these interactions that result in 100-fold difference in binding affinities between the DADMe-ImmA and ImmA analogs.
		+
		+	Neutron structures of the Helicobacter pylori 5'-methylthioadenosine nucleosidase highlight proton sharing and protonation states.,Banco MT, Mishra V, Ostermann A, Schrader TE, Evans GB, Kovalevsky A, Ronning DR Proc Natl Acad Sci U S A. 2016 Nov 29;113(48):13756-13761. Epub 2016 Nov 16. PMID:27856757<ref>PMID:27856757</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5jpc" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 03:27, 10 December 2016

2016-12-10T03:27:49Z

←Older revision		Revision as of 03:27, 10 December 2016
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5jpc is ~~ON HOLD until Paper Publication~~	+	==Joint X-ray/neutron structure of MTAN complex with Formycin A==
-		+	<StructureSection load='5jpc' size='340' side='right' caption='[[5jpc]], [[Resolution\|resolution]] 2.50Å' scene=''>
-	~~Authors~~: ~~Banco~~, M.T., ~~Ronning~~, D.R., ~~Kovalevsky~~, A.Y.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5jpc]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JPC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JPC FirstGlance]. <br>
-	~~Description~~: ~~Joint X-ray~~/~~neutron structure~~ of ~~MTAN complex with Formycin A~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</scene>, <scene name='pdbligand=FMC:(1S)-1-(7-AMINO-1H-PYRAZOLO[4,3-D]PYRIMIDIN-3-YL)-1,4-ANHYDRO-D-RIBITOL'>FMC</scene></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5k1z\|5k1z]]</td></tr>
-	[[Category: Kovalevsky, A.Y]]	+	<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=5jpc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jpc OCA], [http://pdbe.org/5jpc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jpc RCSB], [http://www.ebi.ac.uk/pdbsum/5jpc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jpc ProSAT]</span></td></tr>
-	[[Category: Ronning, D.R]]	+	</table>
-	[[Category: ~~Banco, M.T~~]]	+	== Function ==
		+	[[http://www.uniprot.org/uniprot/MQMTN_HELPJ MQMTN_HELPJ]] Catalyzes the direct conversion of aminodeoxyfutalosine (AFL) into dehypoxanthine futalosine (DHFL) and adenine via the hydrolysis of the N-glycosidic bond; this reaction seems to represent an essential step in the menaquinone biosynthesis pathway in Helicobacter species. Also catalyzes the hydrolysis of 5'-methylthioadenosine (MTA) to adenine and 5'-methylthioribose. Can also probably use S-adenosylhomocysteine (SAH) as substrate, leading to adenine and S-ribosylhomocysteine. These other activities highlight the tremendous versatility of the enzyme, which also plays key roles in S-adenosylmethionine recycling and in the biosynthesis of the quorum-sensing molecule autoinducer-2.<ref>PMID:20954236</ref> <ref>PMID:22891633</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Banco, M T]]
		+	[[Category: Kovalevsky, A Y]]
		+	[[Category: Ronning, D R]]
		+	[[Category: Helicobacter pylori]]
		+	[[Category: Hydrolase]]
		+	[[Category: Joint neutron and x-ray]]
		+	[[Category: Neutron]]
		+	[[Category: Nucleosidase]]

OCA at 11:36, 26 July 2016

2016-07-26T11:36:18Z

←Older revision		Revision as of 11:36, 26 July 2016
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5jpc is ON HOLD	+	The entry 5jpc is ON HOLD until Paper Publication

	Authors: Banco, M.T., Ronning, D.R., Kovalevsky, A.Y.		Authors: Banco, M.T., Ronning, D.R., Kovalevsky, A.Y.

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

2016-05-15T15:42:07Z

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

←Older revision

Revision as of 15:42, 15 May 2016

OCA: New page: '''Unreleased structure''' The entry 5jpc is ON HOLD Authors: Banco, M.T., Ronning, D.R., Kovalevsky, A.Y. Description: Joint X-ray/neutron structure of MTAN complex with Formycin A [[...

2016-05-15T15:42:05Z

New page: '''Unreleased structure''' The entry 5jpc is ON HOLD Authors: Banco, M.T., Ronning, D.R., Kovalevsky, A.Y. Description: Joint X-ray/neutron structure of MTAN complex with Formycin A [[...

New page

'''Unreleased structure'''

The entry 5jpc is ON HOLD

Authors: Banco, M.T., Ronning, D.R., Kovalevsky, A.Y.

Description: Joint X-ray/neutron structure of MTAN complex with Formycin A
[[Category: Unreleased Structures]]
[[Category: Kovalevsky, A.Y]]
[[Category: Ronning, D.R]]
[[Category: Banco, M.T]]