2w4l
From Proteopedia
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==HUMAN DCMP DEAMINASE== | ==HUMAN DCMP DEAMINASE== | ||
<StructureSection load='2w4l' size='340' side='right' caption='[[2w4l]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='2w4l' size='340' side='right' caption='[[2w4l]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2w4l]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2w4l]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W4L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2W4L FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/dCMP_deaminase dCMP deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.12 3.5.4.12] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/dCMP_deaminase dCMP deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.12 3.5.4.12] </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=2w4l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w4l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2w4l RCSB], [http://www.ebi.ac.uk/pdbsum/2w4l 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=2w4l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w4l OCA], [http://pdbe.org/2w4l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2w4l RCSB], [http://www.ebi.ac.uk/pdbsum/2w4l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2w4l ProSAT]</span></td></tr> |
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
| - | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2w4l ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
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| + | ==See Also== | ||
| + | *[[Deaminase|Deaminase]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Human]] |
[[Category: DCMP deaminase]] | [[Category: DCMP deaminase]] | ||
[[Category: Arrowsmith, C H]] | [[Category: Arrowsmith, C H]] | ||
Revision as of 18:20, 11 August 2016
HUMAN DCMP DEAMINASE
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Categories: Human | DCMP deaminase | Arrowsmith, C H | Berg, S Van Den | Berglund, H | Bountra, C | Collins, R | Dahlgren, L G | Edwards, A M | Flodin, S | Flores, A | Graslund, S | Hammarstrom, M | Johansson, A | Johansson, I | Karlberg, T | Kotenyova, T | Lehtio, L | Moche, M | Nilsson, M E | Nordlund, P | Nyman, T | Persson, C | Sagemark, J | Schuler, H | Siponen, M I | Thorsell, A G | Tresaugues, L | Weigelt, J | Welin, M | Wikstrom, M | Wisniewska, M | Allosteric enzyme | Hexamer | Hydrolase | Metal-binding | Nucleotide biosynthesis | Phosphoprotein | Pyrimidine metabolism
