2h5a
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, resolution 1.72Å | |||||||
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Ligands: | , , | ||||||
Gene: | algC (Pseudomonas aeruginosa) | ||||||
Related: | 1K35, 1K2Y, 1P5D, 1P5G, 1PCJ, 1PCM, 2H4L
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Complex of the enzyme PMM/PGM with xylose 1-phosphate
OverviewOverview
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.
About this StructureAbout this Structure
2H5A is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.
ReferenceReference
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
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