1yd3
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1yd3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YD3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YD3 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1yd3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YD3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YD3 FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ln0|1ln0]], [[1mk0|1mk0]], [[1kft|1kft]], [[1d9x|1d9x]], [[1ycz|1ycz]], [[1yd0|1yd0]], [[1yd1|1yd1]], [[1yd2|1yd2]], [[1yd4|1yd4]], [[1yd5|1yd5]], [[1yd6|1yd6]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ln0|1ln0]], [[1mk0|1mk0]], [[1kft|1kft]], [[1d9x|1d9x]], [[1ycz|1ycz]], [[1yd0|1yd0]], [[1yd1|1yd1]], [[1yd2|1yd2]], [[1yd4|1yd4]], [[1yd5|1yd5]], [[1yd6|1yd6]]</td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yd3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yd3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1yd3 RCSB], [http://www.ebi.ac.uk/pdbsum/1yd3 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=1yd3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yd3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1yd3 RCSB], [http://www.ebi.ac.uk/pdbsum/1yd3 PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/UVRC_THEMA UVRC_THEMA]] The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision (By similarity). | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 33: | Line 35: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
| - | [[Category: Croteau, D L | + | [[Category: Croteau, D L]] |
| - | [[Category: DellaVecchia, M J | + | [[Category: DellaVecchia, M J]] |
| - | [[Category: Houten, B Van | + | [[Category: Houten, B Van]] |
| - | [[Category: Karakas, E | + | [[Category: Karakas, E]] |
| - | [[Category: Kisker, C | + | [[Category: Kisker, C]] |
| - | [[Category: Rhau, B | + | [[Category: Rhau, B]] |
| - | [[Category: Skorvaga, M | + | [[Category: Skorvaga, M]] |
| - | [[Category: Truglio, J J | + | [[Category: Truglio, J J]] |
| - | [[Category: Wang, H | + | [[Category: Wang, H]] |
| - | [[Category: Wang, L | + | [[Category: Wang, L]] |
[[Category: Dna binding protein]] | [[Category: Dna binding protein]] | ||
Revision as of 12:10, 25 December 2014
Crystal structure of the GIY-YIG N-terminal endonuclease domain of UvrC from Thermotoga maritima: Point mutant Y43F bound to its catalytic divalent cation
| |||||||||||
