5er1

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Current revision (11:44, 6 November 2024) (edit) (undo)
 
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<StructureSection load='5er1' size='340' side='right'caption='[[5er1]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='5er1' size='340' side='right'caption='[[5er1]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5er1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Crypa Crypa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ER1 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5ER1 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5er1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cryphonectria_parasitica Cryphonectria parasitica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ER1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ER1 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0HT:METHYL+N-[(2S,3S)-3-AMINO-2-HYDROXY-5-METHYLHEXYL]-L-VALYL-L-ISOLEUCYL-L-PHENYLALANINATE'>0HT</scene></td></tr>
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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&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.103, 3.4.23.18, 3.4.23.19, 3.4.23.20, 3.4.23.21, 3.4.23.22, 3.4.23.23, 3.4.23.24, 3.4.23.25, 3.4.23.26, 3.4.23.28 and 3.4.23.30 3.4.21.103, 3.4.23.18, 3.4.23.19, 3.4.23.20, 3.4.23.21, 3.4.23.22, 3.4.23.23, 3.4.23.24, 3.4.23.25, 3.4.23.26, 3.4.23.28 and 3.4.23.30] </span></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=0HT:METHYL+N-[(2S,3S)-3-AMINO-2-HYDROXY-5-METHYLHEXYL]-L-VALYL-L-ISOLEUCYL-L-PHENYLALANINATE'>0HT</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5er1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5er1 OCA], [http://pdbe.org/5er1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5er1 RCSB], [http://www.ebi.ac.uk/pdbsum/5er1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5er1 ProSAT]</span></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=5er1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5er1 OCA], [https://pdbe.org/5er1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5er1 RCSB], [https://www.ebi.ac.uk/pdbsum/5er1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5er1 ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CARP_CRYPA CARP_CRYPA]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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<jmolCheckbox>
<jmolCheckbox>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/er/5er1_consurf.spt"</scriptWhenChecked>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/er/5er1_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
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Yeast enolase (2-phospho-D-glycerate hydrolyase, EC 4.2.1.11) has been crystallized by vapor diffusion and equilibrium dialysis of solutions of ammonium sulfate. The crystals with the dimer have 2-fold axial symmetry and appear to be suitable for high-resolution X-ray diffraction analysis. Our potential heavy-atom derivative of the native crystals has been prepared.
Yeast enolase (2-phospho-D-glycerate hydrolyase, EC 4.2.1.11) has been crystallized by vapor diffusion and equilibrium dialysis of solutions of ammonium sulfate. The crystals with the dimer have 2-fold axial symmetry and appear to be suitable for high-resolution X-ray diffraction analysis. Our potential heavy-atom derivative of the native crystals has been prepared.
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Crystallization and preliminary crystallographic data for a tetragonal form of yeast enolase.,Lebioda L, Brewer JM J Mol Biol. 1984 Nov 25;180(1):213-5. PMID:6392568<ref>PMID:6392568</ref>
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Crystallization and preliminary crystallographic data for a tetragonal form of yeast enolase.,Lebioda L, Brewer JM J Mol Biol. 1984 Nov 25;180(1):213-5. PMID:006392568<ref>PMID:006392568</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Crypa]]
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[[Category: Cryphonectria parasitica]]
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[[Category: Hydrolase]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Blundell, T L]]
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[[Category: Blundell TL]]
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[[Category: Cooper, J B]]
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[[Category: Cooper JB]]
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[[Category: Foundling, S I]]
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[[Category: Foundling SI]]
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[[Category: Acid proteinase]]
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[[Category: Hydrolase-hydrolase inhibitor complex]]
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Current revision

A rational approach to the design of antihypertensives. X-ray studies of complexes between aspartic proteinases and aminoalcohol renin inhibitors

PDB ID 5er1

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