3vpo
From Proteopedia
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==Crystal structure of human ribonucleotide reductase subunit M2 (hRRM2) mutant== | ==Crystal structure of human ribonucleotide reductase subunit M2 (hRRM2) mutant== | ||
<StructureSection load='3vpo' size='340' side='right' caption='[[3vpo]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='3vpo' size='340' side='right' caption='[[3vpo]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3vpo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3vpo]] is a 2 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=3VPO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VPO FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3olj|3olj]], [[3vpm|3vpm]], [[3vpn|3vpn]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3olj|3olj]], [[3vpm|3vpm]], [[3vpn|3vpn]]</td></tr> | ||
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RR2, RRM2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RR2, RRM2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> |
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribonucleoside-diphosphate_reductase Ribonucleoside-diphosphate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.4.1 1.17.4.1] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribonucleoside-diphosphate_reductase Ribonucleoside-diphosphate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.4.1 1.17.4.1] </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=3vpo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vpo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vpo RCSB], [http://www.ebi.ac.uk/pdbsum/3vpo 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=3vpo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vpo OCA], [http://pdbe.org/3vpo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3vpo RCSB], [http://www.ebi.ac.uk/pdbsum/3vpo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3vpo ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Human]] |
[[Category: Ribonucleoside-diphosphate reductase]] | [[Category: Ribonucleoside-diphosphate reductase]] | ||
[[Category: Chen, B]] | [[Category: Chen, B]] | ||
Revision as of 09:43, 5 August 2016
Crystal structure of human ribonucleotide reductase subunit M2 (hRRM2) mutant
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Categories: Human | Ribonucleoside-diphosphate reductase | Chen, B | Chen, X | Liu, H | Shao, J | Xu, Z | Yang, C | Zhang, L | Zhu, L | Zhu, W | Metal-binding | Oxidoreductase
