2h4l

Complex of PMM/PGM with ribose 1-phosphateComplex of PMM/PGM with ribose 1-phosphate

Structural highlights 2h4l is a 1 chain structure with sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: , NonStd Res: Related: 1k35, 1p5d, 1p5g, 1pcj, 1pcm, 1k2y, 2h5a Gene: algC (Pseudomonas aeruginosa) Resources: FirstGlance, OCA, RCSB, PDBsum 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 Two complexes of the enzyme phosphomannomutase/phosphoglucomutase (PMM/PGM) from Pseudomonas aeruginosa with a slow substrate and with an inhibitor have been characterized by X-ray crystallography. Both ligands induce an interdomain rearrangement in the enzyme that creates a highly buried active site. Comparisons with enzyme-substrate complexes show that the inhibitor xylose 1-phosphate utilizes many of the previously observed enzyme-ligand interactions. In contrast, analysis of the ribose 1-phosphate complex reveals a combination of new and conserved enzyme-ligand interactions for binding. The ability of PMM/PGM to accommodate these two pentose phosphosugars in its active site may be relevant for future efforts towards inhibitor design. Complexes of the enzyme phosphomannomutase/phosphoglucomutase with a slow substrate and an inhibitor.,Regni C, Shackelford GS, Beamer LJ Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Aug 1;62(Pt, 8):722-6. Epub 2006 Jul 24. PMID:16880541 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Phosphomannomutase

spinqualitylabelsall models 2h4l, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image