1hcb: Difference between revisions

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New page: left|200px<br /> <applet load="1hcb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hcb, resolution 1.6Å" /> '''ENZYME-SUBSTRATE INT...
 
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[[Image:1hcb.gif|left|200px]]<br />
<applet load="1hcb" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1hcb, resolution 1.6&Aring;" />
'''ENZYME-SUBSTRATE INTERACTIONS: STRUCTURE OF HUMAN CARBONIC ANHYDRASE I COMPLEXED WITH BICARBONATE'''<br />


==Overview==
==ENZYME-SUBSTRATE INTERACTIONS: STRUCTURE OF HUMAN CARBONIC ANHYDRASE I COMPLEXED WITH BICARBONATE==
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.
<StructureSection load='1hcb' size='340' side='right'caption='[[1hcb]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
<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>
</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/hc/1hcb_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=1hcb ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
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].
*[[Carbonic anhydrase 3D structures|Carbonic anhydrase 3D structures]]
 
== References ==
==Reference==
<references/>
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]
__TOC__
[[Category: Carbonate dehydratase]]
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Kannan, K.K.]]
[[Category: Kannan KK]]
[[Category: Kumar, V.]]
[[Category: Kumar V]]
[[Category: BCT]]
[[Category: ZN]]
[[Category: lyase(oxo-acid)]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:15:33 2007''

Latest revision as of 10:27, 7 February 2024

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

Structural highlights

1hcb is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.6Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CAH1_HUMAN Reversible hydration of carbon dioxide. Can hydrates cyanamide to urea.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Briganti F, Mangani S, Scozzafava A, Vernaglione G, Supuran CT. Carbonic anhydrase catalyzes cyanamide hydration to urea: is it mimicking the physiological reaction? J Biol Inorg Chem. 1999 Oct;4(5):528-36. PMID:10550681

1hcb, resolution 1.60Å

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