3hyf: Difference between revisions

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<StructureSection load='3hyf' size='340' side='right'caption='[[3hyf]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='3hyf' size='340' side='right'caption='[[3hyf]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<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>
<table><tr><td colspan='2'>[[3hyf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. 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" 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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
<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='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='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'>[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>
<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>
== Function ==
[https://www.uniprot.org/uniprot/RNH_ECOLI RNH_ECOLI] Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. RNase H participates in DNA replication; it helps to specify the origin of genomic replication by suppressing initiation at origins other than the oriC locus; along with the 5'-3' exonuclease of pol1, it removes RNA primers from the Okazaki fragments of lagging strand synthesis; and it defines the origin of replication for ColE1-type plasmids by specific cleavage of an RNA preprimer.[HAMAP-Rule:MF_00042][https://www.uniprot.org/uniprot/Q72547_9HIV1 Q72547_9HIV1]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Human immunodeficiency virus 1]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Ribonuclease H]]
[[Category: Kirschberg TA]]
[[Category: Kirschberg, T A]]
[[Category: Lansdon EB]]
[[Category: Lansdon, E B]]
[[Category: Aspartyl protease]]
[[Category: Di-valent metal coordination]]
[[Category: Di-valent metal nucleic acid cleavage mechanism]]
[[Category: Dna integration]]
[[Category: Dna recombination]]
[[Category: Endonuclease]]
[[Category: Hiv-1]]
[[Category: Hydrolase]]
[[Category: Magnesium]]
[[Category: Metal-binding]]
[[Category: Multifunctional enzyme]]
[[Category: Nuclease]]
[[Category: Nucleotidyltransferase]]
[[Category: Protease]]
[[Category: Rna-directed dna polymerase]]
[[Category: Rnase h]]
[[Category: Transferase]]

Revision as of 07:33, 6 September 2023

Crystal structure of HIV-1 RNase H p15 with engineered E. coli loop and active site inhibitor

3hyf, resolution 1.70Å

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