3kbb: Difference between revisions
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<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=3kbb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kbb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3kbb RCSB], [http://www.ebi.ac.uk/pdbsum/3kbb 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=3kbb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kbb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3kbb RCSB], [http://www.ebi.ac.uk/pdbsum/3kbb PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/P1254_THEMA P1254_THEMA]] Displays high phosphatase activity toward erythrose 4-phosphate, fructose 6-phosphate, 2-deoxyglucose 6-phosphate, and mannose 6-phosphate. May have a role in the intracellular metabolism of many phosphorylated carbohydrates. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 18:20, 24 December 2014
Crystal structure of putative beta-phosphoglucomutase from Thermotoga maritimaCrystal structure of putative beta-phosphoglucomutase from Thermotoga maritima
Structural highlights
Function[P1254_THEMA] Displays high phosphatase activity toward erythrose 4-phosphate, fructose 6-phosphate, 2-deoxyglucose 6-phosphate, and mannose 6-phosphate. May have a role in the intracellular metabolism of many phosphorylated carbohydrates. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe structure of TM1254, a putative beta-phosphoglucomutase from T. maritima, was determined to 1.74 A resolution in a high-throughput structural genomics programme. Diffraction data were obtained from crystals belonging to space group P22(1)2(1), with unit-cell parameters a = 48.16, b = 66.70, c = 83.80 A, and were refined to an R factor of 19.2%. The asymmetric unit contained one protein molecule which is comprised of two domains. Structural homologues were found from protein databases that confirmed a strong resemblance between TM1254 and members of the haloacid dehalogenase (HAD) hydrolase family. Structure of a putative beta-phosphoglucomutase (TM1254) from Thermotoga maritima.,Strange RW, Antonyuk SV, Ellis MJ, Bessho Y, Kuramitsu S, Shinkai A, Yokoyama S, Hasnain SS Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Dec 1;65(Pt, 12):1218-21. Epub 2009 Nov 27. PMID:20054115[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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