3kbb

Crystal structure of putative beta-phosphoglucomutase from Thermotoga maritima

spinqualitylabelsall models 3kbb, resolution 1.74Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3kbb is a 1 chain structure with sequence from Thema. This structure supersedes the now removed PDB entry 2pib. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL, SO4 NonStd Res: MSE Gene: bpgm, tm_1254 (THEMA) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 PubMed The 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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