1hcb

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[[Image:1hcb.gif|left|200px]]
[[Image:1hcb.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1hcb |SIZE=350|CAPTION= <scene name='initialview01'>1hcb</scene>, resolution 1.6&Aring;
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The line below this paragraph, containing "STRUCTURE_1hcb", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=BCT:BICARBONATE+ION'>BCT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <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>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1hcb| PDB=1hcb | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hcb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hcb OCA], [http://www.ebi.ac.uk/pdbsum/1hcb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hcb RCSB]</span>
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}}
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'''ENZYME-SUBSTRATE INTERACTIONS: STRUCTURE OF HUMAN CARBONIC ANHYDRASE I COMPLEXED WITH BICARBONATE'''
'''ENZYME-SUBSTRATE INTERACTIONS: STRUCTURE OF HUMAN CARBONIC ANHYDRASE I COMPLEXED WITH BICARBONATE'''
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[[Category: Kannan, K K.]]
[[Category: Kannan, K K.]]
[[Category: Kumar, V.]]
[[Category: Kumar, V.]]
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[[Category: lyase(oxo-acid)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:41:28 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:02:11 2008''
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Revision as of 15:41, 2 May 2008

Image:1hcb.gif

Template:STRUCTURE 1hcb

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


Overview

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.

About this Structure

1HCB is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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:8057362 Page seeded by OCA on Fri May 2 18:41:28 2008

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