2wq7: Difference between revisions
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<StructureSection load='2wq7' size='340' side='right'caption='[[2wq7]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='2wq7' size='340' side='right'caption='[[2wq7]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2wq7]] is a 3 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2wq7]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WQ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WQ7 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=TDY:5-(METHYLAMINO)THYMIDINE+5-(DIHYDROGEN+PHOSPHATE)'>TDY</scene>, <scene name='pdbligand=Z:1-(2-DEOXY-5-O-PHOSPHONO-BETA-D-ERYTHRO-PENTOFURANOSYL)PYRIMIDIN-2(1H)-ONE'>Z</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=2wq7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wq7 OCA], [https://pdbe.org/2wq7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wq7 RCSB], [https://www.ebi.ac.uk/pdbsum/2wq7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wq7 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8SXK5_DROME Q8SXK5_DROME] | |||
== 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: | [[Category: Drosophila melanogaster]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Carell | [[Category: Carell T]] | ||
[[Category: Glas | [[Category: Glas AF]] | ||
[[Category: Kaya | [[Category: Kaya E]] | ||
[[Category: Maul | [[Category: Maul MJ]] | ||
[[Category: Schneider | [[Category: Schneider S]] | ||
Latest revision as of 13:13, 20 December 2023
Structure of the 6-4 photolyase of D. melanogaster in complex with the non-natural N4-methyl T(6-4)C lesionStructure of the 6-4 photolyase of D. melanogaster in complex with the non-natural N4-methyl T(6-4)C lesion
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedRepair of the Dewar valence isomers by (6-4) photolyases proceeds via an enzyme catalyzed ring-opening reaction of the Dewar lesion to the (6-4) photoproduct. DNA (6-4) Photolyases Reduce Dewar Isomers for Isomerization into (6-4) Lesions.,Glas AF, Kaya E, Schneider S, Heil K, Fazio D, Maul MJ, Carell T J Am Chem Soc. 2010 Feb 18. PMID:20166732[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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