4lu3

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<StructureSection load='4lu3' size='340' side='right' caption='[[4lu3]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='4lu3' size='340' side='right' caption='[[4lu3]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4lu3]] 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=4LU3 OCA]. <br>
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<table><tr><td colspan='2'>[[4lu3]] 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=4LU3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LU3 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AZM:5-ACETAMIDO-1,3,4-THIADIAZOLE-2-SULFONAMIDE'>AZM</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene><br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AZM:5-ACETAMIDO-1,3,4-THIADIAZOLE-2-SULFONAMIDE'>AZM</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CA14, UNQ690/PRO1335 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CA14, UNQ690/PRO1335 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
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<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>
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<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=4lu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lu3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lu3 RCSB], [http://www.ebi.ac.uk/pdbsum/4lu3 PDBsum]</span></td></tr>
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<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=4lu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lu3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lu3 RCSB], [http://www.ebi.ac.uk/pdbsum/4lu3 PDBsum]</span></td></tr>
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<table>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/CAH14_HUMAN CAH14_HUMAN]] Reversible hydration of carbon dioxide.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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The structural comparison between membrane-associated human carbonic anhydrases provides insights into drug design of selective inhibitors.,Alterio V, Pan P, Parkkila S, Buonanno M, Supuran CT, Monti SM, De Simone G Biopolymers. 2014 Jul;101(7):769-78. doi: 10.1002/bip.22456. PMID:24374484<ref>PMID:24374484</ref>
The structural comparison between membrane-associated human carbonic anhydrases provides insights into drug design of selective inhibitors.,Alterio V, Pan P, Parkkila S, Buonanno M, Supuran CT, Monti SM, De Simone G Biopolymers. 2014 Jul;101(7):769-78. doi: 10.1002/bip.22456. PMID:24374484<ref>PMID:24374484</ref>
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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==See Also==
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*[[Carbonic anhydrase|Carbonic anhydrase]]
== References ==
== References ==
<references/>
<references/>
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[[Category: Carbonate dehydratase]]
[[Category: Carbonate dehydratase]]
[[Category: Human]]
[[Category: Human]]
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[[Category: Alterio, V.]]
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[[Category: Alterio, V]]
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[[Category: Monti, S M.]]
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[[Category: Monti, S M]]
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[[Category: Simone, G De.]]
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[[Category: Simone, G De]]
[[Category: Glycoprotein]]
[[Category: Glycoprotein]]
[[Category: Lyase-lyase inhibitor complex]]
[[Category: Lyase-lyase inhibitor complex]]
[[Category: Membrane]]
[[Category: Membrane]]
[[Category: Zinc binding]]
[[Category: Zinc binding]]

Revision as of 20:18, 24 December 2014

The crystal structure of the human carbonic anhydrase XIV

4lu3, resolution 2.00Å

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