1i9o - Revision history

OCA at 07:33, 7 February 2024

2024-02-07T07:33:20Z

←Older revision		Revision as of 07:33, 7 February 2024
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	<StructureSection load='1i9o' size='340' side='right'caption='[[1i9o]], [[Resolution\|resolution]] 1.86Å' scene=''>		<StructureSection load='1i9o' size='340' side='right'caption='[[1i9o]], [[Resolution\|resolution]] 1.86Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1i9o]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I9O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I9O FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1i9o]] 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=1I9O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I9O FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=IOC:4-(AMINOSULFONYL)-N-[(2,3,4-TRIFLUOROPHENYL)METHYL]-BENZAMIDE'>IOC</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]] 1.86Å</td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1i9l\|1i9l]], [[1i9m\|1i9m]], [[1i9n\|1i9n]], [[1i9p\|1i9p]], [[1i9q\|1i9q]], [[1g1d\|1g1d]], [[1g52\|1g52]], [[1g53\|1g53]], [[1g54\|1g54]], [[1g3z\|1g3z]], [[1g4o\|1g4o]], [[1g45\|1g45]], [[1g46\|1g46]], [[1g48\|1g48]], [[1g4j\|1g4j]]</div></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=IOC:4-(AMINOSULFONYL)-N-[(2,3,4-TRIFLUOROPHENYL)METHYL]-BENZAMIDE'>IOC</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Carbonate_dehydratase Carbonate dehydratase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=1i9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i9o OCA], [https://pdbe.org/1i9o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i9o RCSB], [https://www.ebi.ac.uk/pdbsum/1i9o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i9o 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=1i9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i9o OCA], [https://pdbe.org/1i9o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i9o RCSB], [https://www.ebi.ac.uk/pdbsum/1i9o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i9o ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[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>	+	[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 ==
-	[[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>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1i9o ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1i9o ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Intermolecular interactions of eleven different fluoroaromatic inhibitors are probed within the scaffolding of the crystal lattice of Phe-131-->Val carbonic anhydrase II. The degree and pattern of fluorine substitution on the inhibitor benzyl ring modulate its size, shape, and electronic character. In turn, these properties affect the geometry of intermolecular interactions between the fluoroaromatic rings of two different inhibitor molecules bound in the crystal lattice, as determined by X-ray crystallography. Depending on the degree and pattern of fluorine substitution, we observe a face-to-face (aromatic-aromatic) interaction, an atom-to-face (carbonyl-aromatic) interaction, or no interaction at all. These interaction geometries are analyzed with regard to van der Waals, electrostatic, and possible charge-transfer effects. For the aromatic-aromatic interactions investigated in this study, with aromatic ring quadrupoles specifically "tuned" by the degree and pattern of fluorination, the structural results suggest that London forces and charge-transfer complexation dominate over weakly polar electrostatic interactions in the association of aromatic ring pairs.
-
-	Fluoroaromatic-fluoroaromatic interactions between inhibitors bound in the crystal lattice of human carbonic anhydrase II.,Kim CY, Chandra PP, Jain A, Christianson DW J Am Chem Soc. 2001 Oct 3;123(39):9620-7. PMID:11572683<ref>PMID:11572683</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1i9o" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 39:		Line 29:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Carbonate dehydratase]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Chandra~~, P P~~]]	+	[[Category: Chandra PP]]
-	[[Category: Christianson~~, D W~~]]	+	[[Category: Christianson DW]]
-	[[Category: Jain, A]]	+	[[Category: Jain A]]
-	[[Category: Kim, C Y]]	+	[[Category: Kim C-Y]]
-	~~[[Category: Human carbonic anhydrase ii]]~~	+
-	~~[[Category: Lyase~~]]	+

OCA at 13:14, 13 October 2021

2021-10-13T13:14:03Z

OCA at 10:14, 8 January 2020

2020-01-08T10:14:05Z

←Older revision		Revision as of 10:14, 8 January 2020
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	==CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(2,3,4-TRIFLUOROPHENYL)METHYL]-BENZAMIDE==		==CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(2,3,4-TRIFLUOROPHENYL)METHYL]-BENZAMIDE==
-	<StructureSection load='1i9o' size='340' side='right' caption='[[1i9o]], [[Resolution\|resolution]] 1.86Å' scene=''>	+	<StructureSection load='1i9o' size='340' side='right'caption='[[1i9o]], [[Resolution\|resolution]] 1.86Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1i9o]] 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=1I9O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1I9O FirstGlance]. <br>		<table><tr><td colspan='2'>[[1i9o]] 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=1I9O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1I9O FirstGlance]. <br>
Line 34:		Line 34:

	==See Also==		==See Also==
-	*[[Carbonic anhydrase\|Carbonic anhydrase]]	+	*[[Carbonic anhydrase 3D structures\|Carbonic anhydrase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 41:		Line 41:
	[[Category: Carbonate dehydratase]]		[[Category: Carbonate dehydratase]]
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Chandra, P P]]		[[Category: Chandra, P P]]
	[[Category: Christianson, D W]]		[[Category: Christianson, D W]]

OCA at 06:14, 4 April 2018

2018-04-04T06:14:08Z

←Older revision		Revision as of 06:14, 4 April 2018
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	</div>		</div>
	<div class="pdbe-citations 1i9o" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1i9o" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Carbonic anhydrase\|Carbonic anhydrase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 09:02, 10 January 2018

2018-01-10T09:02:58Z

←Older revision		Revision as of 09:02, 10 January 2018
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		+
	==CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(2,3,4-TRIFLUOROPHENYL)METHYL]-BENZAMIDE==		==CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(2,3,4-TRIFLUOROPHENYL)METHYL]-BENZAMIDE==
	<StructureSection load='1i9o' size='340' side='right' caption='[[1i9o]], [[Resolution\|resolution]] 1.86Å' scene=''>		<StructureSection load='1i9o' size='340' side='right' caption='[[1i9o]], [[Resolution\|resolution]] 1.86Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1i9l\|1i9l]], [[1i9m\|1i9m]], [[1i9n\|1i9n]], [[1i9p\|1i9p]], [[1i9q\|1i9q]], [[1g1d\|1g1d]], [[1g52\|1g52]], [[1g53\|1g53]], [[1g54\|1g54]], [[1g3z\|1g3z]], [[1g4o\|1g4o]], [[1g45\|1g45]], [[1g46\|1g46]], [[1g48\|1g48]], [[1g4j\|1g4j]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1i9l\|1i9l]], [[1i9m\|1i9m]], [[1i9n\|1i9n]], [[1i9p\|1i9p]], [[1i9q\|1i9q]], [[1g1d\|1g1d]], [[1g52\|1g52]], [[1g53\|1g53]], [[1g54\|1g54]], [[1g3z\|1g3z]], [[1g4o\|1g4o]], [[1g45\|1g45]], [[1g46\|1g46]], [[1g48\|1g48]], [[1g4j\|1g4j]]</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=1i9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i9o OCA], [http://pdbe.org/1i9o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1i9o RCSB], [http://www.ebi.ac.uk/pdbsum/1i9o 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=1i9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i9o OCA], [http://pdbe.org/1i9o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1i9o RCSB], [http://www.ebi.ac.uk/pdbsum/1i9o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1i9o ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i9/1i9o_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i9/1i9o_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
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	</div>		</div>
	<div class="pdbe-citations 1i9o" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1i9o" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Carbonic anhydrase\|Carbonic anhydrase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 02:30, 9 February 2016

2016-02-09T02:30:11Z

←Older revision		Revision as of 02:30, 9 February 2016
Line 20:		Line 20:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1i9o ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 17:44, 10 September 2015

2015-09-10T17:44:07Z

←Older revision		Revision as of 17:44, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1i9o' size='340' side='right' caption='[[1i9o]], [[Resolution\|resolution]] 1.86Å' scene=''>		<StructureSection load='1i9o' size='340' side='right' caption='[[1i9o]], [[Resolution\|resolution]] 1.86Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1i9o]] is a 1 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=1I9O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1I9O FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1i9o]] 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=1I9O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1I9O FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=IOC:4-(AMINOSULFONYL)-N-[(2,3,4-TRIFLUOROPHENYL)METHYL]-BENZAMIDE'>IOC</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=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=IOC:4-(AMINOSULFONYL)-N-[(2,3,4-TRIFLUOROPHENYL)METHYL]-BENZAMIDE'>IOC</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">[[1i9l\|1i9l]], [[1i9m\|1i9m]], [[1i9n\|1i9n]], [[1i9p\|1i9p]], [[1i9q\|1i9q]], [[1g1d\|1g1d]], [[1g52\|1g52]], [[1g53\|1g53]], [[1g54\|1g54]], [[1g3z\|1g3z]], [[1g4o\|1g4o]], [[1g45\|1g45]], [[1g46\|1g46]], [[1g48\|1g48]], [[1g4j\|1g4j]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1i9l\|1i9l]], [[1i9m\|1i9m]], [[1i9n\|1i9n]], [[1i9p\|1i9p]], [[1i9q\|1i9q]], [[1g1d\|1g1d]], [[1g52\|1g52]], [[1g53\|1g53]], [[1g54\|1g54]], [[1g3z\|1g3z]], [[1g4o\|1g4o]], [[1g45\|1g45]], [[1g46\|1g46]], [[1g48\|1g48]], [[1g4j\|1g4j]]</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=1i9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i9o OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1i9o RCSB], [http://www.ebi.ac.uk/pdbsum/1i9o 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=1i9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i9o OCA], [http://pdbe.org/1i9o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1i9o RCSB], [http://www.ebi.ac.uk/pdbsum/1i9o PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
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	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 1i9o" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 38:		Line 39:
	</StructureSection>		</StructureSection>
	[[Category: Carbonate dehydratase]]		[[Category: Carbonate dehydratase]]
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Chandra, P P]]		[[Category: Chandra, P P]]
	[[Category: Christianson, D W]]		[[Category: Christianson, D W]]

OCA at 09:40, 2 January 2015

2015-01-02T09:40:48Z

←Older revision		Revision as of 09:40, 2 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1i9o]] is a 1 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=1I9O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1I9O FirstGlance]. <br>		<table><tr><td colspan='2'>[[1i9o]] is a 1 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=1I9O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1I9O FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=IOC:4-(AMINOSULFONYL)-N-[(2,3,4-TRIFLUOROPHENYL)METHYL]-BENZAMIDE'>IOC</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=IOC:4-(AMINOSULFONYL)-N-[(2,3,4-TRIFLUOROPHENYL)METHYL]-BENZAMIDE'>IOC</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1i9l\|1i9l]], [[1i9m\|1i9m]], [[1i9n\|1i9n]], [[1i9p\|1i9p]], [[1i9q\|1i9q]], [[1g1d\|1g1d]], [[1g52\|1g52]], [[1g53\|1g53]], [[1g54\|1g54]], [[1g3z\|1g3z]], [[1g4o\|1g4o]], [[1g45\|1g45]], [[1g46\|1g46]], [[1g48\|1g48]], [[1g4j\|1g4j]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1i9l\|1i9l]], [[1i9m\|1i9m]], [[1i9n\|1i9n]], [[1i9p\|1i9p]], [[1i9q\|1i9q]], [[1g1d\|1g1d]], [[1g52\|1g52]], [[1g53\|1g53]], [[1g54\|1g54]], [[1g3z\|1g3z]], [[1g4o\|1g4o]], [[1g45\|1g45]], [[1g46\|1g46]], [[1g48\|1g48]], [[1g4j\|1g4j]]</td></tr>
-	<tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1i9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i9o OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1i9o RCSB], [http://www.ebi.ac.uk/pdbsum/1i9o 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=1i9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i9o OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1i9o RCSB], [http://www.ebi.ac.uk/pdbsum/1i9o PDBsum]</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>		[[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>
Line 39:		Line 39:
	[[Category: Carbonate dehydratase]]		[[Category: Carbonate dehydratase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Chandra, P P.]]	+	[[Category: Chandra, P P]]
-	[[Category: Christianson, D W.]]	+	[[Category: Christianson, D W]]
-	[[Category: Jain, A.]]	+	[[Category: Jain, A]]
-	[[Category: Kim, C Y.]]	+	[[Category: Kim, C Y]]
	[[Category: Human carbonic anhydrase ii]]		[[Category: Human carbonic anhydrase ii]]
	[[Category: Lyase]]		[[Category: Lyase]]

OCA at 14:59, 29 September 2014

2014-09-29T14:59:31Z

←Older revision		Revision as of 14:59, 29 September 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_1i9o\| PDB=1i9o \| SCENE= }}~~	+	==CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(2,3,4-TRIFLUOROPHENYL)METHYL]-BENZAMIDE==
-	===CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(2,3,4-TRIFLUOROPHENYL)METHYL]-BENZAMIDE===	+	<StructureSection load='1i9o' size='340' side='right' caption='[[1i9o]], [[Resolution\|resolution]] 1.86Å' scene=''>
-	~~{{ABSTRACT_PUBMED_11572683}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1i9o]] is a 1 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=1I9O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1I9O FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=IOC:4-(AMINOSULFONYL)-N-[(2,3,4-TRIFLUOROPHENYL)METHYL]-BENZAMIDE'>IOC</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1i9l\|1i9l]], [[1i9m\|1i9m]], [[1i9n\|1i9n]], [[1i9p\|1i9p]], [[1i9q\|1i9q]], [[1g1d\|1g1d]], [[1g52\|1g52]], [[1g53\|1g53]], [[1g54\|1g54]], [[1g3z\|1g3z]], [[1g4o\|1g4o]], [[1g45\|1g45]], [[1g46\|1g46]], [[1g48\|1g48]], [[1g4j\|1g4j]]</td></tr>
		+	<tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1i9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i9o OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1i9o RCSB], [http://www.ebi.ac.uk/pdbsum/1i9o 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>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i9/1i9o_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Intermolecular interactions of eleven different fluoroaromatic inhibitors are probed within the scaffolding of the crystal lattice of Phe-131-->Val carbonic anhydrase II. The degree and pattern of fluorine substitution on the inhibitor benzyl ring modulate its size, shape, and electronic character. In turn, these properties affect the geometry of intermolecular interactions between the fluoroaromatic rings of two different inhibitor molecules bound in the crystal lattice, as determined by X-ray crystallography. Depending on the degree and pattern of fluorine substitution, we observe a face-to-face (aromatic-aromatic) interaction, an atom-to-face (carbonyl-aromatic) interaction, or no interaction at all. These interaction geometries are analyzed with regard to van der Waals, electrostatic, and possible charge-transfer effects. For the aromatic-aromatic interactions investigated in this study, with aromatic ring quadrupoles specifically "tuned" by the degree and pattern of fluorination, the structural results suggest that London forces and charge-transfer complexation dominate over weakly polar electrostatic interactions in the association of aromatic ring pairs.

-	~~==Disease==~~	+	Fluoroaromatic-fluoroaromatic interactions between inhibitors bound in the crystal lattice of human carbonic anhydrase II.,Kim CY, Chandra PP, Jain A, Christianson DW J Am Chem Soc. 2001 Oct 3;123(39):9620-7. PMID:11572683<ref>PMID:11572683</ref>
-	~~[[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==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[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>
-		+
-	~~==About this Structure==~~	+
-	[[1i9o]] is a 1 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=1I9O OCA].	+

	==See Also==		==See Also==
	*[[Carbonic anhydrase\|Carbonic anhydrase]]		*[[Carbonic anhydrase\|Carbonic anhydrase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:011572683</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Carbonate dehydratase]]		[[Category: Carbonate dehydratase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

OCA at 01:11, 25 March 2013

2013-03-25T01:11:59Z

←Older revision		Revision as of 01:11, 25 March 2013
Line 1:		Line 1:
-	[[Image:1i9o.png\|left\|200px]]
-
	{{STRUCTURE_1i9o\| PDB=1i9o \| SCENE= }}		{{STRUCTURE_1i9o\| PDB=1i9o \| SCENE= }}
-
	===CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(2,3,4-TRIFLUOROPHENYL)METHYL]-BENZAMIDE===		===CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(2,3,4-TRIFLUOROPHENYL)METHYL]-BENZAMIDE===
		+	{{ABSTRACT_PUBMED_11572683}}

-	~~{{ABSTRACT_PUBMED_11572683}}~~	+	==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>

	==About this Structure==		==About this Structure==
Line 14:		Line 16:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:011572683</ref><references group="xtra"/>	+	<ref group="xtra">PMID:011572683</ref><references group="xtra"/><references/>
	[[Category: Carbonate dehydratase]]		[[Category: Carbonate dehydratase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

←Older revision		Revision as of 13:14, 13 October 2021
Line 3:		Line 3:
	<StructureSection load='1i9o' size='340' side='right'caption='[[1i9o]], [[Resolution\|resolution]] 1.86Å' scene=''>		<StructureSection load='1i9o' size='340' side='right'caption='[[1i9o]], [[Resolution\|resolution]] 1.86Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1i9o]] 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=1I9O OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1I9O FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1i9o]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I9O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I9O FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=IOC:4-(AMINOSULFONYL)-N-[(2,3,4-TRIFLUOROPHENYL)METHYL]-BENZAMIDE'>IOC</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=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=IOC:4-(AMINOSULFONYL)-N-[(2,3,4-TRIFLUOROPHENYL)METHYL]-BENZAMIDE'>IOC</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">[[1i9l\|1i9l]], [[1i9m\|1i9m]], [[1i9n\|1i9n]], [[1i9p\|1i9p]], [[1i9q\|1i9q]], [[1g1d\|1g1d]], [[1g52\|1g52]], [[1g53\|1g53]], [[1g54\|1g54]], [[1g3z\|1g3z]], [[1g4o\|1g4o]], [[1g45\|1g45]], [[1g46\|1g46]], [[1g48\|1g48]], [[1g4j\|1g4j]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1i9l\|1i9l]], [[1i9m\|1i9m]], [[1i9n\|1i9n]], [[1i9p\|1i9p]], [[1i9q\|1i9q]], [[1g1d\|1g1d]], [[1g52\|1g52]], [[1g53\|1g53]], [[1g54\|1g54]], [[1g3z\|1g3z]], [[1g4o\|1g4o]], [[1g45\|1g45]], [[1g46\|1g46]], [[1g48\|1g48]], [[1g4j\|1g4j]]</div></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'>[https://en.wikipedia.org/wiki/Carbonate_dehydratase Carbonate dehydratase], with EC number [https://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=1i9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i9o OCA], [~~http~~://pdbe.org/1i9o PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1i9o RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1i9o PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1i9o 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=1i9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i9o OCA], [https://pdbe.org/1i9o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i9o RCSB], [https://www.ebi.ac.uk/pdbsum/1i9o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i9o 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>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]