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==Crystal structure of Glycerate kinase (EC 2.7.1.31) (tm1585) from THERMOTOGA MARITIMA at 2.70 A resolution==
==Crystal structure of Glycerate kinase (EC 2.7.1.31) (tm1585) from THERMOTOGA MARITIMA at 2.70 A resolution==
<StructureSection load='2b8n' size='340' side='right' caption='[[2b8n]], [[Resolution|resolution]] 2.53&Aring;' scene=''>
<StructureSection load='2b8n' size='340' side='right'caption='[[2b8n]], [[Resolution|resolution]] 2.53&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2b8n]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1o0u 1o0u]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B8N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2B8N FirstGlance]. <br>
<table><tr><td colspan='2'>[[2b8n]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1o0u 1o0u]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B8N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B8N FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tm1585 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima])</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=2b8n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b8n OCA], [https://pdbe.org/2b8n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b8n RCSB], [https://www.ebi.ac.uk/pdbsum/2b8n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b8n ProSAT], [https://www.topsan.org/Proteins/JCSG/2b8n TOPSAN]</span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glycerate_kinase Glycerate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.31 2.7.1.31] </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=2b8n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b8n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2b8n RCSB], [http://www.ebi.ac.uk/pdbsum/2b8n PDBsum], [http://www.topsan.org/Proteins/JCSG/2b8n TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/Q9X1S1_THEMA Q9X1S1_THEMA]] Involved in the degradation of serine via 3-hydroxypyruvate. Catalyzes the ATP-dependent phosphorylation of D-glycerate to 2-phosphoglycerate.<ref>PMID:18156253</ref>
[https://www.uniprot.org/uniprot/GCK_THEMA GCK_THEMA] Involved in the degradation of serine via 3-hydroxypyruvate. Catalyzes the ATP-dependent phosphorylation of D-glycerate to 2-phosphoglycerate.<ref>PMID:18156253</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b8/2b8n_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b8/2b8n_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <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/chain_selection.php?pdb_ID=2ata ConSurf].
</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=2b8n ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
==See Also==
*[[Glycerate kinase|Glycerate kinase]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Glycerate kinase]]
[[Category: Large Structures]]
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima MSB8]]
[[Category: Structural genomic]]
[[Category: Jcsg]]
[[Category: PSI, Protein structure initiative]]
[[Category: Tm1585]]
[[Category: Transferase]]

Latest revision as of 09:43, 25 January 2023

Crystal structure of Glycerate kinase (EC 2.7.1.31) (tm1585) from THERMOTOGA MARITIMA at 2.70 A resolutionCrystal structure of Glycerate kinase (EC 2.7.1.31) (tm1585) from THERMOTOGA MARITIMA at 2.70 A resolution

Structural highlights

2b8n is a 2 chain structure with sequence from Thermotoga maritima MSB8. This structure supersedes the now removed PDB entry 1o0u. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

GCK_THEMA Involved in the degradation of serine via 3-hydroxypyruvate. Catalyzes the ATP-dependent phosphorylation of D-glycerate to 2-phosphoglycerate.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Yang C, Rodionov DA, Rodionova IA, Li X, Osterman AL. Glycerate 2-kinase of Thermotoga maritima and genomic reconstruction of related metabolic pathways. J Bacteriol. 2008 Mar;190(5):1773-82. Epub 2007 Dec 21. PMID:18156253 doi:http://dx.doi.org/10.1128/JB.01469-07

2b8n, resolution 2.53Å

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