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1hcb

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(New page: 200px<br /> <applet load="1hcb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hcb, resolution 1.6&Aring;" /> '''ENZYME-SUBSTRATE INT...)
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[[Image:1hcb.gif|left|200px]]<br />
 
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<applet load="1hcb" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1hcb, resolution 1.6&Aring;" />
 
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'''ENZYME-SUBSTRATE INTERACTIONS: STRUCTURE OF HUMAN CARBONIC ANHYDRASE I COMPLEXED WITH BICARBONATE'''<br />
 
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==Overview==
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==ENZYME-SUBSTRATE INTERACTIONS: STRUCTURE OF HUMAN CARBONIC ANHYDRASE I COMPLEXED WITH BICARBONATE==
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The structure of HCAI-HCO3- complex has been refined with 10-1.6A X-ray, diffraction data to an R-value of 17.7%. The structure reveals monodentate, binding of the HCO3- anion at an apical tetrahedral position to the zinc, ion. The binding mode and interactions of HCO3- in HCAI differ from that, in HCAII. The activity linked H2O/OH- group in the free HCAI is replaced, by the hydroxyl group of the bicarbonate anion. This result rules out the, rearrangement of the bound HCO3- advocated earlier to explain the, microscopic reversibility of the catalysed reaction. From the geometry of, the H-bonds between Glu106-Thr199 pair and Glu117-His119 couple, the, glutamic acids are expected to be ionized and accept H-bonds from their, partners. The product-inhibiton by HCO3- anion is explained on the basis, of proton localization on His119 in the Glu117-His119 couple. These, results are consistent with the hypothesis that Glu117-His119 tunes the, ionicity of the Zn2+ and the binding strength of HCO3- anion. A pi, hydrogen bond is observed between a water and phenyl ring of the Tyr114, residue.
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<StructureSection load='1hcb' size='340' side='right'caption='[[1hcb]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1hcb]] 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=1HCB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HCB FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCT:BICARBONATE+ION'>BCT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hcb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hcb OCA], [https://pdbe.org/1hcb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hcb RCSB], [https://www.ebi.ac.uk/pdbsum/1hcb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hcb ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CAH1_HUMAN CAH1_HUMAN] Reversible hydration of carbon dioxide. Can hydrates cyanamide to urea.<ref>PMID:10550681</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hc/1hcb_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1hcb ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1HCB 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 and BCT as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1HCB OCA].
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*[[Carbonic anhydrase 3D structures|Carbonic anhydrase 3D structures]]
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== References ==
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==Reference==
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<references/>
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Enzyme-substrate interactions. Structure of human carbonic anhydrase I complexed with bicarbonate., Kumar V, Kannan KK, J Mol Biol. 1994 Aug 12;241(2):226-32. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8057362 8057362]
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__TOC__
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[[Category: Carbonate dehydratase]]
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Kannan, K.K.]]
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[[Category: Kannan KK]]
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[[Category: Kumar, V.]]
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[[Category: Kumar V]]
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[[Category: BCT]]
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[[Category: ZN]]
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[[Category: lyase(oxo-acid)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:15:33 2007''
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Current revision

ENZYME-SUBSTRATE INTERACTIONS: STRUCTURE OF HUMAN CARBONIC ANHYDRASE I COMPLEXED WITH BICARBONATE

PDB ID 1hcb

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