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1gha

From Proteopedia

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(New page: 200px<br /><applet load="1gha" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gha, resolution 2.2&Aring;" /> '''A SECOND ACTIVE SITE ...)
Current revision (11:21, 27 March 2024) (edit) (undo)
 
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[[Image:1gha.gif|left|200px]]<br /><applet load="1gha" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1gha, resolution 2.2&Aring;" />
 
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'''A SECOND ACTIVE SITE IN CHYMOTRYPSIN? THE X-RAY CRYSTAL STRUCTURE OF N-ACETYL-D-TRYPTOPHAN BOUND TO GAMMA-CHYMOTRYPSIN'''<br />
 
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==About this Structure==
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==A SECOND ACTIVE SITE IN CHYMOTRYPSIN? THE X-RAY CRYSTAL STRUCTURE OF N-ACETYL-D-TRYPTOPHAN BOUND TO GAMMA-CHYMOTRYPSIN==
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1GHA is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with SO4 and IPA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Chymotrypsin Chymotrypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.1 3.4.21.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GHA OCA].
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<StructureSection load='1gha' size='340' side='right'caption='[[1gha]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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[[Category: Bos taurus]]
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== Structural highlights ==
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[[Category: Chymotrypsin]]
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<table><tr><td colspan='2'>[[1gha]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GHA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GHA FirstGlance]. <br>
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[[Category: Protein complex]]
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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]] 2.2&#8491;</td></tr>
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[[Category: Farber, G.K.]]
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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[[Category: Yennawar, H.P.]]
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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=1gha FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gha OCA], [https://pdbe.org/1gha PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gha RCSB], [https://www.ebi.ac.uk/pdbsum/1gha PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gha ProSAT]</span></td></tr>
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[[Category: Yennawar, N.H.]]
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</table>
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[[Category: IPA]]
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== Function ==
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[[Category: SO4]]
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[https://www.uniprot.org/uniprot/CTRA_BOVIN CTRA_BOVIN]
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[[Category: hydrolase(serine proteinase)]]
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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/gh/1gha_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=1gha ConSurf].
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<div style="clear:both"></div>
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:03:27 2007''
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==See Also==
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*[[Chymotrypsin 3D structures|Chymotrypsin 3D structures]]
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__TOC__
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</StructureSection>
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[[Category: Bos taurus]]
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[[Category: Large Structures]]
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[[Category: Farber GK]]
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[[Category: Yennawar HP]]
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[[Category: Yennawar NH]]

Current revision

A SECOND ACTIVE SITE IN CHYMOTRYPSIN? THE X-RAY CRYSTAL STRUCTURE OF N-ACETYL-D-TRYPTOPHAN BOUND TO GAMMA-CHYMOTRYPSIN

PDB ID 1gha

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