2wgh
From Proteopedia
(Difference between revisions)
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==Human Ribonucleotide reductase R1 subunit (RRM1) in complex with dATP and Mg.== | ==Human Ribonucleotide reductase R1 subunit (RRM1) in complex with dATP and Mg.== | ||
- | <StructureSection load='2wgh' size='340' side='right' caption='[[2wgh]], [[Resolution|resolution]] 2.30Å' scene=''> | + | <StructureSection load='2wgh' size='340' side='right'caption='[[2wgh]], [[Resolution|resolution]] 2.30Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[2wgh]] 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=2WGH OCA]. For a <b>guided tour on the structure components</b> use [http:// | + | <table><tr><td colspan='2'>[[2wgh]] 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=2WGH OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2WGH FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DTP:2-DEOXYADENOSINE+5-TRIPHOSPHATE'>DTP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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" id="ligandDat"><scene name='pdbligand=DTP:2-DEOXYADENOSINE+5-TRIPHOSPHATE'>DTP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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:// | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2wgh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wgh OCA], [http://pdbe.org/2wgh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wgh RCSB], [http://www.ebi.ac.uk/pdbsum/2wgh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2wgh ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
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==See Also== | ==See Also== | ||
- | *[[Ribonucleotide reductase|Ribonucleotide reductase]] | + | *[[Ribonucleotide reductase 3D structures|Ribonucleotide reductase 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
+ | [[Category: Large Structures]] | ||
[[Category: Ribonucleoside-diphosphate reductase]] | [[Category: Ribonucleoside-diphosphate reductase]] | ||
[[Category: Arrowsmith, C H]] | [[Category: Arrowsmith, C H]] |
Revision as of 08:41, 1 July 2020
Human Ribonucleotide reductase R1 subunit (RRM1) in complex with dATP and Mg.
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Categories: Human | Large Structures | Ribonucleoside-diphosphate reductase | Arrowsmith, C H | Berg, S Van Den | Berglund, H | Bountra, C | Collins, R | Edwards, A M | Flodin, S | Flores, A | Graslund, S | Hammarstrom, M | Johansson, A | Johansson, I | Karlberg, T | Kotenyova, T | Kotzsch, A | Kragh-Nielsen, T | Moche, M | Nordlund, P | Nyman, T | Persson, C | Sagemark, J | Schueler, H | Schutz, P | Siponen, M I | Svensson, L | Thorsell, A G | Tresaugues, L | Weigelt, J | Welin, R M | Wisniewska, M | Allosteric enzyme | Atp-binding | Cytoplasm | Dna replication | Nucleotide-binding | Oxidoreductase | Polymorphism