5ehv - Revision history

OCA at 12:28, 6 March 2024

2024-03-06T12:28:36Z

←Older revision		Revision as of 12:28, 6 March 2024
Line 12:		Line 12:
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/CAH2_HUMAN CAH2_HUMAN] Essential for bone resorption and osteoclast differentiation (By similarity). Reversible hydration of carbon dioxide. Can hydrate cyanamide to urea. Involved in the regulation of fluid secretion into the anterior chamber of the eye.<ref>PMID:10550681</ref> <ref>PMID:11831900</ref>		[https://www.uniprot.org/uniprot/CAH2_HUMAN CAH2_HUMAN] Essential for bone resorption and osteoclast differentiation (By similarity). Reversible hydration of carbon dioxide. Can hydrate cyanamide to urea. Involved in the regulation of fluid secretion into the anterior chamber of the eye.<ref>PMID:10550681</ref> <ref>PMID:11831900</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Fragment-based drug discovery (FBDD) is contingent on the development of analytical methods to identify weak protein-fragment noncovalent interactions. Herein we have combined an underutilized fragment screening method, native state mass spectrometry, together with two proven and popular fragment screening methods, surface plasmon resonance and X-ray crystallography, in a fragment screening campaign against human carbonic anhydrase II (CA II). In an initial fragment screen against a 720-member fragment library (the "CSIRO Fragment Library") seven CA II binding fragments, including a selection of nonclassical CA II binding chemotypes, were identified. A further 70 compounds that comprised the initial hit chemotypes were subsequently sourced from the full CSIRO compound collection and screened. The fragment results were extremely well correlated across the three methods. Our findings demonstrate that there is a tremendous opportunity to apply native state mass spectrometry as a complementary fragment screening method to accelerate drug discovery.
-
-	Native State Mass Spectrometry, Surface Plasmon Resonance, and X-ray Crystallography Correlate Strongly as a Fragment Screening Combination.,Woods LA, Dolezal O, Ren B, Ryan JH, Peat TS, Poulsen SA J Med Chem. 2016 Feb 29. PMID:26882437<ref>PMID:26882437</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 5ehv" style="background-color:#fffaf0;"></div>

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

OCA at 06:28, 5 July 2023

2023-07-05T06:28:43Z

←Older revision		Revision as of 06:28, 5 July 2023
Line 3:		Line 3:
	<StructureSection load='5ehv' size='340' side='right'caption='[[5ehv]], [[Resolution\|resolution]] 1.21Å' scene=''>		<StructureSection load='5ehv' size='340' side='right'caption='[[5ehv]], [[Resolution\|resolution]] 1.21Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5ehv]] 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=5EHV OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5EHV FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5ehv]] 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=5EHV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EHV FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5ON:(~{E})-3-[3-[[3-(2-HYDROXY-2-OXOETHYL)PHENYL]METHOXY]PHENYL]PROP-2-ENOIC+ACID'>5ON</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 1.208Å</td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5eh5\|5eh5]], [[5eh7\|5eh7]], [[5eh8\|5eh8]], [[5ehw\|5ehw]], [[5flo\|5flo]], [[5flp\|5flp]], [[5flq\|5flq]], [[5flr\|5flr]], [[5fls\|5fls]], [[5flt\|5flt]], [[5fng\|5fng]], [[5fnh\|5fnh]], [[5fni\|5fni]], [[5fnj\|5fnj]], [[5fnk\|5fnk]], [[5fnm\|5fnm]]</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5ON:(~{E})-3-[3-[[3-(2-HYDROXY-2-OXOETHYL)PHENYL]METHOXY]PHENYL]PROP-2-ENOIC+ACID'>5ON</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CA2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>~~	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ehv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ehv OCA], [https://pdbe.org/5ehv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ehv RCSB], [https://www.ebi.ac.uk/pdbsum/5ehv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ehv ProSAT]</span></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carbonate_dehydratase Carbonate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.1 4.2.1.1] </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=5ehv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ehv OCA], [~~http~~://pdbe.org/5ehv PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5ehv RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5ehv PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5ehv ProSAT]</span></td></tr>	+
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/CAH2_HUMAN CAH2_HUMAN]] Defects in CA2 are the cause of osteopetrosis autosomal recessive type 3 (OPTB3) [MIM:[~~http~~://omim.org/entry/259730 259730]]; also known as osteopetrosis with renal tubular acidosis, carbonic anhydrase II deficiency syndrome, Guibaud-Vainsel syndrome or marble brain disease. Osteopetrosis is a rare genetic disease characterized by abnormally dense bone, due to defective resorption of immature bone. The disorder occurs in two forms: a severe autosomal recessive form occurring in utero, infancy, or childhood, and a benign autosomal dominant form occurring in adolescence or adulthood. Autosomal recessive osteopetrosis is usually associated with normal or elevated amount of non-functional osteoclasts. OPTB3 is associated with renal tubular acidosis, cerebral calcification (marble brain disease) and in some cases with mental retardation.<ref>PMID:1928091</ref> <ref>PMID:1542674</ref> <ref>PMID:8834238</ref> <ref>PMID:9143915</ref> <ref>PMID:15300855</ref>	+	[https://www.uniprot.org/uniprot/CAH2_HUMAN CAH2_HUMAN] Defects in CA2 are the cause of osteopetrosis autosomal recessive type 3 (OPTB3) [MIM:[https://omim.org/entry/259730 259730]; also known as osteopetrosis with renal tubular acidosis, carbonic anhydrase II deficiency syndrome, Guibaud-Vainsel syndrome or marble brain disease. Osteopetrosis is a rare genetic disease characterized by abnormally dense bone, due to defective resorption of immature bone. The disorder occurs in two forms: a severe autosomal recessive form occurring in utero, infancy, or childhood, and a benign autosomal dominant form occurring in adolescence or adulthood. Autosomal recessive osteopetrosis is usually associated with normal or elevated amount of non-functional osteoclasts. OPTB3 is associated with renal tubular acidosis, cerebral calcification (marble brain disease) and in some cases with mental retardation.<ref>PMID:1928091</ref> <ref>PMID:1542674</ref> <ref>PMID:8834238</ref> <ref>PMID:9143915</ref> <ref>PMID:15300855</ref>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/CAH2_HUMAN CAH2_HUMAN]] Essential for bone resorption and osteoclast differentiation (By similarity). Reversible hydration of carbon dioxide. Can hydrate cyanamide to urea. Involved in the regulation of fluid secretion into the anterior chamber of the eye.<ref>PMID:10550681</ref> <ref>PMID:11831900</ref>	+	[https://www.uniprot.org/uniprot/CAH2_HUMAN CAH2_HUMAN] Essential for bone resorption and osteoclast differentiation (By similarity). Reversible hydration of carbon dioxide. Can hydrate cyanamide to urea. Involved in the regulation of fluid secretion into the anterior chamber of the eye.<ref>PMID:10550681</ref> <ref>PMID:11831900</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 30:		Line 28:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Carbonate dehydratase]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Ren, B]]	+	[[Category: Ren B]]
-	~~[[Category: Human carbonic anhydrase ii]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 06:58, 22 April 2020

2020-04-22T06:58:52Z

←Older revision		Revision as of 06:58, 22 April 2020
Line 1:		Line 1:

	==human carbonic anhydrase II in complex with ligand==		==human carbonic anhydrase II in complex with ligand==
-	<StructureSection load='5ehv' size='340' side='right' caption='[[5ehv]], [[Resolution\|resolution]] 1.21Å' scene=''>	+	<StructureSection load='5ehv' size='340' side='right'caption='[[5ehv]], [[Resolution\|resolution]] 1.21Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5ehv]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EHV OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5EHV FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5ehv]] 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=5EHV OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5EHV FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5ON:(~{E})-3-[3-[[3-(2-HYDROXY-2-OXOETHYL)PHENYL]METHOXY]PHENYL]PROP-2-ENOIC+ACID'>5ON</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=5ON:(~{E})-3-[3-[[3-(2-HYDROXY-2-OXOETHYL)PHENYL]METHOXY]PHENYL]PROP-2-ENOIC+ACID'>5ON</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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">[[5eh5\|5eh5]], [[5eh7\|5eh7]], [[5eh8\|5eh8]], [[5ehw\|5ehw]], [[5flo\|5flo]], [[5flp\|5flp]], [[5flq\|5flq]], [[5flr\|5flr]], [[5fls\|5fls]], [[5flt\|5flt]], [[5fng\|5fng]], [[5fnh\|5fnh]], [[5fni\|5fni]], [[5fnj\|5fnj]], [[5fnk\|5fnk]], [[5fnm\|5fnm]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5eh5\|5eh5]], [[5eh7\|5eh7]], [[5eh8\|5eh8]], [[5ehw\|5ehw]], [[5flo\|5flo]], [[5flp\|5flp]], [[5flq\|5flq]], [[5flr\|5flr]], [[5fls\|5fls]], [[5flt\|5flt]], [[5fng\|5fng]], [[5fnh\|5fnh]], [[5fni\|5fni]], [[5fnj\|5fnj]], [[5fnk\|5fnk]], [[5fnm\|5fnm]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CA2 ([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/Carbonate_dehydratase Carbonate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.1 4.2.1.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carbonate_dehydratase Carbonate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.1 4.2.1.1] </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=5ehv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ehv OCA], [http://pdbe.org/5ehv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ehv RCSB], [http://www.ebi.ac.uk/pdbsum/5ehv PDBsum]</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=5ehv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ehv OCA], [http://pdbe.org/5ehv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ehv RCSB], [http://www.ebi.ac.uk/pdbsum/5ehv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ehv ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 22:		Line 23:
	</div>		</div>
	<div class="pdbe-citations 5ehv" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5ehv" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Carbonic anhydrase 3D structures\|Carbonic anhydrase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 27:		Line 31:
	</StructureSection>		</StructureSection>
	[[Category: Carbonate dehydratase]]		[[Category: Carbonate dehydratase]]
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Ren, B]]		[[Category: Ren, B]]
	[[Category: Human carbonic anhydrase ii]]		[[Category: Human carbonic anhydrase ii]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 03:33, 10 March 2016

2016-03-10T03:33:57Z

←Older revision		Revision as of 03:33, 10 March 2016
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5ehv is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==human carbonic anhydrase II in complex with ligand==
		+	<StructureSection load='5ehv' size='340' side='right' caption='[[5ehv]], [[Resolution\|resolution]] 1.21Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5ehv]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EHV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EHV FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5ON:(~{E})-3-[3-[[3-(2-HYDROXY-2-OXOETHYL)PHENYL]METHOXY]PHENYL]PROP-2-ENOIC+ACID'>5ON</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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">[[5eh5\|5eh5]], [[5eh7\|5eh7]], [[5eh8\|5eh8]], [[5ehw\|5ehw]], [[5flo\|5flo]], [[5flp\|5flp]], [[5flq\|5flq]], [[5flr\|5flr]], [[5fls\|5fls]], [[5flt\|5flt]], [[5fng\|5fng]], [[5fnh\|5fnh]], [[5fni\|5fni]], [[5fnj\|5fnj]], [[5fnk\|5fnk]], [[5fnm\|5fnm]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carbonate_dehydratase Carbonate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.1 4.2.1.1] </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=5ehv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ehv OCA], [http://pdbe.org/5ehv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ehv RCSB], [http://www.ebi.ac.uk/pdbsum/5ehv PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/CAH2_HUMAN CAH2_HUMAN]] Defects in CA2 are the cause of osteopetrosis autosomal recessive type 3 (OPTB3) [MIM:[http://omim.org/entry/259730 259730]]; also known as osteopetrosis with renal tubular acidosis, carbonic anhydrase II deficiency syndrome, Guibaud-Vainsel syndrome or marble brain disease. Osteopetrosis is a rare genetic disease characterized by abnormally dense bone, due to defective resorption of immature bone. The disorder occurs in two forms: a severe autosomal recessive form occurring in utero, infancy, or childhood, and a benign autosomal dominant form occurring in adolescence or adulthood. Autosomal recessive osteopetrosis is usually associated with normal or elevated amount of non-functional osteoclasts. OPTB3 is associated with renal tubular acidosis, cerebral calcification (marble brain disease) and in some cases with mental retardation.<ref>PMID:1928091</ref> <ref>PMID:1542674</ref> <ref>PMID:8834238</ref> <ref>PMID:9143915</ref> <ref>PMID:15300855</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/CAH2_HUMAN CAH2_HUMAN]] Essential for bone resorption and osteoclast differentiation (By similarity). Reversible hydration of carbon dioxide. Can hydrate cyanamide to urea. Involved in the regulation of fluid secretion into the anterior chamber of the eye.<ref>PMID:10550681</ref> <ref>PMID:11831900</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Fragment-based drug discovery (FBDD) is contingent on the development of analytical methods to identify weak protein-fragment noncovalent interactions. Herein we have combined an underutilized fragment screening method, native state mass spectrometry, together with two proven and popular fragment screening methods, surface plasmon resonance and X-ray crystallography, in a fragment screening campaign against human carbonic anhydrase II (CA II). In an initial fragment screen against a 720-member fragment library (the "CSIRO Fragment Library") seven CA II binding fragments, including a selection of nonclassical CA II binding chemotypes, were identified. A further 70 compounds that comprised the initial hit chemotypes were subsequently sourced from the full CSIRO compound collection and screened. The fragment results were extremely well correlated across the three methods. Our findings demonstrate that there is a tremendous opportunity to apply native state mass spectrometry as a complementary fragment screening method to accelerate drug discovery.

-	~~Authors: Ren~~, B.	+	Native State Mass Spectrometry, Surface Plasmon Resonance, and X-ray Crystallography Correlate Strongly as a Fragment Screening Combination.,Woods LA, Dolezal O, Ren B, Ryan JH, Peat TS, Poulsen SA J Med Chem. 2016 Feb 29. PMID:26882437<ref>PMID:26882437</ref>

-	~~Description~~: ~~human carbonic anhydrase II in complex with ligand~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased Structures~~]]	+	</div>
		+	<div class="pdbe-citations 5ehv" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Carbonate dehydratase]]
	[[Category: Ren, B]]		[[Category: Ren, B]]
		+	[[Category: Human carbonic anhydrase ii]]
		+	[[Category: Transferase]]

OCA at 14:41, 2 December 2015

2015-12-02T14:41:10Z

←Older revision		Revision as of 14:41, 2 December 2015
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors: Ren, B.		Authors: Ren, B.

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

2015-12-01T02:51:55Z

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

←Older revision

Revision as of 02:51, 1 December 2015

OCA: New page: '''Unreleased structure''' The entry 5ehv is ON HOLD Authors: Ren, B. Description: human carbonic anhydrase II in complex with ligand Category: Unreleased Structures [[Category: Re...

2015-12-01T02:51:54Z

New page: '''Unreleased structure''' The entry 5ehv is ON HOLD Authors: Ren, B. Description: human carbonic anhydrase II in complex with ligand Category: Unreleased Structures [[Category: Re...

New page

'''Unreleased structure'''

The entry 5ehv is ON HOLD

Authors: Ren, B.

Description: human carbonic anhydrase II in complex with ligand
[[Category: Unreleased Structures]]
[[Category: Ren, B]]