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3hyf
From Proteopedia
(Difference between revisions)
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==Crystal structure of HIV-1 RNase H p15 with engineered E. coli loop and active site inhibitor== | ==Crystal structure of HIV-1 RNase H p15 with engineered E. coli loop and active site inhibitor== | ||
| - | <StructureSection load='3hyf' size='340' side='right' caption='[[3hyf]], [[Resolution|resolution]] 1.70Å' scene=''> | + | <StructureSection load='3hyf' size='340' side='right'caption='[[3hyf]], [[Resolution|resolution]] 1.70Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3hyf]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3hyf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/9hiv1 9hiv1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HYF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HYF FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=ON1:2-(3,4-DICHLOROBENZYL)-5,6-DIHYDROXYPYRIMIDINE-4-CARBOXYLIC+ACID'>ON1</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=ON1:2-(3,4-DICHLOROBENZYL)-5,6-DIHYDROXYPYRIMIDINE-4-CARBOXYLIC+ACID'>ON1</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pol, Reverse Transcriptase (amino acids 427-560) ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pol, Reverse Transcriptase (amino acids 427-560) ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11676 9HIV1]), b0214, dasF, herA, JW0204, rnh, rnhA, sdrA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11676 9HIV1]), pol ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11676 9HIV1])</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ribonuclease_H Ribonuclease H], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.26.4 3.1.26.4] </span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3hyf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hyf OCA], [https://pdbe.org/3hyf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hyf RCSB], [https://www.ebi.ac.uk/pdbsum/3hyf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hyf ProSAT]</span></td></tr> |
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hy/3hyf_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hy/3hyf_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</div> | </div> | ||
<div class="pdbe-citations 3hyf" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3hyf" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Reverse transcriptase 3D structures|Reverse transcriptase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Ribonuclease H]] | [[Category: Ribonuclease H]] | ||
[[Category: Kirschberg, T A]] | [[Category: Kirschberg, T A]] | ||
Revision as of 11:18, 6 April 2022
Crystal structure of HIV-1 RNase H p15 with engineered E. coli loop and active site inhibitor
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Categories: Large Structures | Ribonuclease H | Kirschberg, T A | Lansdon, E B | Aspartyl protease | Di-valent metal coordination | Di-valent metal nucleic acid cleavage mechanism | Dna integration | Dna recombination | Endonuclease | Hiv-1 | Hydrolase | Magnesium | Metal-binding | Multifunctional enzyme | Nuclease | Nucleotidyltransferase | Protease | Rna-directed dna polymerase | Rnase h | Transferase
