2cab: Difference between revisions

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[[Image:2cab.gif|left|200px]]<br />
<applet load="2cab" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2cab, resolution 2.0&Aring;" />
'''STRUCTURE, REFINEMENT AND FUNCTION OF CARBONIC ANHYDRASE ISOZYMES. REFINEMENT OF HUMAN CARBONIC ANHYDRASE I'''<br />


==Overview==
==STRUCTURE, REFINEMENT AND FUNCTION OF CARBONIC ANHYDRASE ISOZYMES. REFINEMENT OF HUMAN CARBONIC ANHYDRASE I==
The structure of human erythrocyte carbonic anhydrase I has been refined, to a final R value of 19% to 2-A resolution by a combination of least, squares refinement and model fitting in a three-dimensional graphics, display. About 300 solvent atoms have been located bound to the protein, molecule. An interesting hydrogen bond network involving Zn2+, the, liganded solvent, side chain groups of Thr-199, Glu-106, Thr-7, and His-64, through two solvent molecules have been found that may be important for, the catalytic mechanism of the carbonic anhydrase.
<StructureSection load='2cab' size='340' side='right'caption='[[2cab]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2cab]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1cab 1cab]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CAB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CAB FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=2cab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cab OCA], [https://pdbe.org/2cab PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cab RCSB], [https://www.ebi.ac.uk/pdbsum/2cab PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cab ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CAH1_HUMAN CAH1_HUMAN] Reversible hydration of carbon dioxide. Can hydrates cyanamide to urea.<ref>PMID:10550681</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/ca/2cab_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/main_output.php?pdb_ID=2cab ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
2CAB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. This structure superseeds the now removed PDB entry 1CAB. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CAB OCA].
*[[Carbonic anhydrase 3D structures|Carbonic anhydrase 3D structures]]
 
== References ==
==Reference==
<references/>
Structure, refinement, and function of carbonic anhydrase isozymes: refinement of human carbonic anhydrase I., Kannan KK, Ramanadham M, Jones TA, Ann N Y Acad Sci. 1984;429:49-60. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=6430186 6430186]
__TOC__
[[Category: Carbonate dehydratase]]
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Jones, T.A.]]
[[Category: Jones TA]]
[[Category: Kannan, K.K.]]
[[Category: Kannan KK]]
[[Category: Ramanadham, M.]]
[[Category: Ramanadham M]]
[[Category: ZN]]
[[Category: hydro-lyase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 21:13:20 2007''

Latest revision as of 09:17, 14 February 2024

STRUCTURE, REFINEMENT AND FUNCTION OF CARBONIC ANHYDRASE ISOZYMES. REFINEMENT OF HUMAN CARBONIC ANHYDRASE I

2cab, resolution 2.00Å

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