6ptv: Difference between revisions

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<StructureSection load='6ptv' size='340' side='right'caption='[[6ptv]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
<StructureSection load='6ptv' size='340' side='right'caption='[[6ptv]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6ptv]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PTV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6PTV FirstGlance]. <br>
<table><tr><td colspan='2'>[[6ptv]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Rickettsia_rickettsii_str._'Sheila_Smith' Rickettsia rickettsii str. 'Sheila Smith'] and [https://en.wikipedia.org/wiki/Streptomyces_griseus Streptomyces griseus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PTV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PTV FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</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]] 1.85&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=MLU:N-METHYL-D-LEUCINE'>MLU</scene>, <scene name='pdbligand=MP8:(4R)-4-METHYL-L-PROLINE'>MP8</scene>, <scene name='pdbligand=MVA:N-METHYLVALINE'>MVA</scene>, <scene name='pdbligand=NZC:N-METHYLIDENE-L-THREONINE'>NZC</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=MLU:N-METHYL-D-LEUCINE'>MLU</scene>, <scene name='pdbligand=MP8:(4R)-4-METHYL-L-PROLINE'>MP8</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MVA:N-METHYLVALINE'>MVA</scene>, <scene name='pdbligand=NZC:N-METHYLIDENE-L-THREONINE'>NZC</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6dlk|6dlk]]</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=6ptv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ptv OCA], [https://pdbe.org/6ptv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ptv RCSB], [https://www.ebi.ac.uk/pdbsum/6ptv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ptv ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ptv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ptv OCA], [http://pdbe.org/6ptv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ptv RCSB], [http://www.ebi.ac.uk/pdbsum/6ptv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ptv ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/A0A0H3AWV3_RICRS A0A0H3AWV3_RICRS]] Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP-independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of replication as well as for processivity of DNA replication.[PIRNR:PIRNR000804]  
[https://www.uniprot.org/uniprot/A0A0H3AWV3_RICRS A0A0H3AWV3_RICRS] Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP-independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of replication as well as for processivity of DNA replication.[PIRNR:PIRNR000804]
 
==See Also==
*[[DNA polymerase 3D structures|DNA polymerase 3D structures]]
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Structural genomic]]
[[Category: Rickettsia rickettsii str. 'Sheila Smith']]
[[Category: Antibiotic]]
[[Category: Streptomyces griseus]]
[[Category: Broad spectrum]]
[[Category: Infectious disease]]
[[Category: Myucobacterium]]
[[Category: Natural product]]
[[Category: Niaid]]
[[Category: Ssgcid]]
[[Category: Streptomyce]]
[[Category: Transferase]]
[[Category: Transferase-antibiotic complex]]

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