4j2a - Revision history

OCA at 12:00, 1 March 2024

OCA — Fri, 01 Mar 2024 12:00:37 GMT

←Older revision		Revision as of 12:00, 1 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4j2a]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_phage_RB69 Escherichia phage RB69]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J2A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4J2A FirstGlance]. <br>		<table><tr><td colspan='2'>[[4j2a]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_phage_RB69 Escherichia phage RB69]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J2A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4J2A FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=TTP:THYMIDINE-5-TRIPHOSPHATE'>TTP</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]] 1.8Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=TTP:THYMIDINE-5-TRIPHOSPHATE'>TTP</scene></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=4j2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j2a OCA], [https://pdbe.org/4j2a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4j2a RCSB], [https://www.ebi.ac.uk/pdbsum/4j2a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4j2a 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=4j2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j2a OCA], [https://pdbe.org/4j2a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4j2a RCSB], [https://www.ebi.ac.uk/pdbsum/4j2a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4j2a ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/DPOL_BPR69 DPOL_BPR69] This polymerase possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single stranded DNA in the 3'- to 5'-direction.		[https://www.uniprot.org/uniprot/DPOL_BPR69 DPOL_BPR69] This polymerase possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single stranded DNA in the 3'- to 5'-direction.
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Internal cavities are a common feature of many proteins, often having profound effects on the dynamics of their interactions with substrate and binding partners. RB69 DNA polymerase (pol) has a hydrophobic cavity right below the nucleotide binding pocket at the tip of highly conserved L415 side chain. Replacement of this residue with Gly or Met in other B family pols resulted in higher mutation rates. When similar substitutions for L415 were introduced into RB69pol, only L415A and L415G had dramatic effects on pre-steady-state kinetic parameters, reducing base selectivity by several hundred fold. On the other hand, the L415M variant behaved like the wild-type. Using a novel tC(o)-tCnitro Forster Resonance Energy Transfer (FRET) assay, we were able to show that the partition of the primer terminus between pol and exonuclease (exo) domains was compromised with the L415A and L415G mutants, but not with the L415M variant. These results could be rationalized by changes in their structures as determined by high resolution X-ray crystallography.

-	Alteration in the cavity size adjacent to the active site of RB69 DNA polymerase changes its conformational dynamics.,Xia S, Wood M, Bradley MJ, De La Cruz EM, Konigsberg WH Nucleic Acids Res. 2013 Oct;41(19):9077-89. doi: 10.1093/nar/gkt674. Epub 2013, Aug 5. PMID:23921641<ref>PMID:23921641</ref>	+	==See Also==
-		+	*[[DNA polymerase 3D structures\|DNA polymerase 3D structures]]
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class~~=~~"pdbe-citations 4j2a" style~~=~~"background-color:#fffaf0;"></div>~~	+
-	~~== References~~ ==	+
-	~~<references/>~~	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 21:26, 16 November 2022

OCA — Wed, 16 Nov 2022 21:26:48 GMT

←Older revision		Revision as of 21:26, 16 November 2022
Line 1:		Line 1:

	==RB69 DNA Polymerase L415A Ternary Complex==		==RB69 DNA Polymerase L415A Ternary Complex==
-	<StructureSection load='4j2a' size='340' side='right' caption='[[4j2a]], [[Resolution\|resolution]] 1.80Å' scene=''>	+	<StructureSection load='4j2a' size='340' side='right'caption='[[4j2a]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4j2a]] is a 3 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Bpr69 Bpr69~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J2A OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4J2A FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4j2a]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_phage_RB69 Escherichia phage RB69]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J2A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4J2A FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=TTP:THYMIDINE-5-TRIPHOSPHATE'>TTP</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=TTP:THYMIDINE-5-TRIPHOSPHATE'>TTP</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4j2b\|4j2b]], [[4j2d\|4j2d]], [[4j2e\|4j2e]]</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=4j2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j2a OCA], [https://pdbe.org/4j2a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4j2a RCSB], [https://www.ebi.ac.uk/pdbsum/4j2a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4j2a ProSAT]</span></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">43 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=12353 BPR69])</td></tr>~~	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] </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=4j2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j2a OCA], [~~http~~://pdbe.org/4j2a PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4j2a RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4j2a PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4j2a ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/DPOL_BPR69 DPOL_BPR69]] This polymerase possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single stranded DNA in the 3'- to 5'-direction.	+	[https://www.uniprot.org/uniprot/DPOL_BPR69 DPOL_BPR69] This polymerase possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single stranded DNA in the 3'- to 5'-direction.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 21:		Line 18:
	</div>		</div>
	<div class="pdbe-citations 4j2a" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4j2a" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[DNA polymerase\|DNA polymerase]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Bpr69~~]]	+	[[Category: Escherichia phage RB69]]
-	[[Category: ~~DNA-directed DNA polymerase~~]]	+	[[Category: Large Structures]]
-	[[Category: Konigsberg~~, W H~~]]	+	[[Category: Konigsberg WH]]
-	[[Category: Wang, J]]	+	[[Category: Wang J]]
-	[[Category: Xia, S]]	+	[[Category: Xia S]]
-	~~[[Category: Dna polymerase]]~~	+
-	~~[[Category: L415a]]~~	+
-	~~[[Category: Polymerase]]~~	+
-	~~[[Category: Rb69]]~~	+
-	~~[[Category: Transferase-dna complex~~]]	+

OCA at 17:38, 4 August 2016

OCA — Thu, 04 Aug 2016 17:38:53 GMT

←Older revision		Revision as of 17:38, 4 August 2016
Line 1:		Line 1:
		+
	==RB69 DNA Polymerase L415A Ternary Complex==		==RB69 DNA Polymerase L415A Ternary Complex==
	<StructureSection load='4j2a' size='340' side='right' caption='[[4j2a]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='4j2a' size='340' side='right' caption='[[4j2a]], [[Resolution\|resolution]] 1.80Å' scene=''>
Line 7:		Line 8:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">43 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=12353 BPR69])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">43 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=12353 BPR69])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] </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=4j2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j2a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4j2a RCSB], [http://www.ebi.ac.uk/pdbsum/4j2a PDBsum]</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=4j2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j2a OCA], [http://pdbe.org/4j2a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4j2a RCSB], [http://www.ebi.ac.uk/pdbsum/4j2a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4j2a ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 4j2a" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 17:42, 24 December 2014

OCA — Wed, 24 Dec 2014 17:42:17 GMT

←Older revision		Revision as of 17:42, 24 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4j2a~~\| ~~PDB~~=4j2a \| ~~SCENE~~= }}	+	==RB69 DNA Polymerase L415A Ternary Complex==
-	===~~RB69 DNA Polymerase L415A Ternary Complex~~===	+	<StructureSection load='4j2a' size='340' side='right' caption='[[4j2a]], [[Resolution\|resolution]] 1.80Å' scene=''>
-	~~{{ABSTRACT_PUBMED_23921641}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4j2a]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpr69 Bpr69]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J2A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4J2A FirstGlance]. <br>
-	==Function==	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=TTP:THYMIDINE-5-TRIPHOSPHATE'>TTP</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4j2b\|4j2b]], [[4j2d\|4j2d]], [[4j2e\|4j2e]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">43 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=12353 BPR69])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] </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=4j2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j2a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4j2a RCSB], [http://www.ebi.ac.uk/pdbsum/4j2a PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
	[[http://www.uniprot.org/uniprot/DPOL_BPR69 DPOL_BPR69]] This polymerase possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single stranded DNA in the 3'- to 5'-direction.		[[http://www.uniprot.org/uniprot/DPOL_BPR69 DPOL_BPR69]] This polymerase possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single stranded DNA in the 3'- to 5'-direction.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Internal cavities are a common feature of many proteins, often having profound effects on the dynamics of their interactions with substrate and binding partners. RB69 DNA polymerase (pol) has a hydrophobic cavity right below the nucleotide binding pocket at the tip of highly conserved L415 side chain. Replacement of this residue with Gly or Met in other B family pols resulted in higher mutation rates. When similar substitutions for L415 were introduced into RB69pol, only L415A and L415G had dramatic effects on pre-steady-state kinetic parameters, reducing base selectivity by several hundred fold. On the other hand, the L415M variant behaved like the wild-type. Using a novel tC(o)-tCnitro Forster Resonance Energy Transfer (FRET) assay, we were able to show that the partition of the primer terminus between pol and exonuclease (exo) domains was compromised with the L415A and L415G mutants, but not with the L415M variant. These results could be rationalized by changes in their structures as determined by high resolution X-ray crystallography.
		+
		+	Alteration in the cavity size adjacent to the active site of RB69 DNA polymerase changes its conformational dynamics.,Xia S, Wood M, Bradley MJ, De La Cruz EM, Konigsberg WH Nucleic Acids Res. 2013 Oct;41(19):9077-89. doi: 10.1093/nar/gkt674. Epub 2013, Aug 5. PMID:23921641<ref>PMID:23921641</ref>

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[4j2a]] is~~ a ~~3 chain structure~~. ~~Full crystallographic information is available from [http://oca~~.~~weizmann~~.~~ac.il~~/~~oca-bin/ocashort?id=4J2A OCA].~~	+	</div>

-	==~~Reference~~==	+	==See Also==
-	~~<ref group~~=~~"xtra">PMID:023921641</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	*[[DNA polymerase\|DNA polymerase]]
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Bpr69]]
	[[Category: DNA-directed DNA polymerase]]		[[Category: DNA-directed DNA polymerase]]
-	[[Category: Konigsberg, W H.]]	+	[[Category: Konigsberg, W H]]
-	[[Category: Wang, J.]]	+	[[Category: Wang, J]]
-	[[Category: Xia, S.]]	+	[[Category: Xia, S]]
	[[Category: Dna polymerase]]		[[Category: Dna polymerase]]
	[[Category: L415a]]		[[Category: L415a]]

OCA at 17:37, 19 February 2014

OCA — Wed, 19 Feb 2014 17:37:54 GMT

←Older revision		Revision as of 17:37, 19 February 2014
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{STRUCTURE_4j2a\| PDB=4j2a \| SCENE= }}
		+	===RB69 DNA Polymerase L415A Ternary Complex===
		+	{{ABSTRACT_PUBMED_23921641}}

-	~~The entry 4j2a is ON HOLD until Paper Publication~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/DPOL_BPR69 DPOL_BPR69]] This polymerase possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single stranded DNA in the 3'- to 5'-direction.

-	~~Authors~~: ~~Xia, S~~.~~, Wang, J~~.~~, Konigsberg, W~~.H.	+	==About this Structure==
		+	[[4j2a]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J2A OCA].

-	~~Description~~: ~~RB69~~ DNA Polymerase ~~L415A Ternary Complex~~	+	==Reference==
		+	<ref group="xtra">PMID:023921641</ref><references group="xtra"/><references/>
		+	[[Category: DNA-directed DNA polymerase]]
		+	[[Category: Konigsberg, W H.]]
		+	[[Category: Wang, J.]]
		+	[[Category: Xia, S.]]
		+	[[Category: Dna polymerase]]
		+	[[Category: L415a]]
		+	[[Category: Polymerase]]
		+	[[Category: Rb69]]
		+	[[Category: Transferase-dna complex]]

OCA at 13:48, 6 March 2013

OCA — Wed, 06 Mar 2013 13:48:19 GMT

←Older revision		Revision as of 13:48, 6 March 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4j2a is ON HOLD	+	The entry 4j2a is ON HOLD until Paper Publication

	Authors: Xia, S., Wang, J., Konigsberg, W.H.		Authors: Xia, S., Wang, J., Konigsberg, W.H.

	Description: RB69 DNA Polymerase L415A Ternary Complex		Description: RB69 DNA Polymerase L415A Ternary Complex

OCA: Protected "4j2a" [edit=sysop:move=sysop]

OCA — Wed, 13 Feb 2013 10:10:04 GMT

Protected "4j2a" [edit=sysop:move=sysop]

←Older revision

Revision as of 10:10, 13 February 2013

OCA: New page: '''Unreleased structure''' The entry 4j2a is ON HOLD Authors: Xia, S., Wang, J., Konigsberg, W.H. Description: RB69 DNA Polymerase L415A Ternary Complex

OCA — Wed, 13 Feb 2013 10:10:03 GMT

New page: '''Unreleased structure''' The entry 4j2a is ON HOLD Authors: Xia, S., Wang, J., Konigsberg, W.H. Description: RB69 DNA Polymerase L415A Ternary Complex

New page

'''Unreleased structure'''

The entry 4j2a is ON HOLD

Authors: Xia, S., Wang, J., Konigsberg, W.H.

Description: RB69 DNA Polymerase L415A Ternary Complex