1PP4
The crystal structure of rhamnogalacturonan acetylesterase in space group P3121
Summary for 1PP4
Entry DOI | 10.2210/pdb1pp4/pdb |
Related | 1DEO 1DEX 1K7C |
Descriptor | Rhamnogalacturonan acetylesterase, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total) |
Functional Keywords | gds(l) hydrolase, hydrolase |
Biological source | Aspergillus aculeatus |
Total number of polymer chains | 2 |
Total formula weight | 50130.59 |
Authors | Molgaard, A.,Larsen, S. (deposition date: 2003-06-16, release date: 2004-03-02, Last modification date: 2024-10-16) |
Primary citation | Molgaard, A.,Larsen, S. Crystal packing in two pH-dependent crystal forms of rhamnogalacturonan acetylesterase. Acta Crystallogr.,Sect.D, 60:472-478, 2004 Cited by PubMed Abstract: The glycoprotein rhamnogalacturonan acetylesterase from Aspergillus aculeatus has been crystallized in two crystal forms, an orthorhombic and a trigonal crystal form. In the orthorhombic crystal form, the covalently bound carbohydrate at one of the two N-glycosylation sites is involved in crystal contacts. The orthorhombic crystal form was obtained at pH 5.0 and the trigonal crystal form at pH 4.5. In one case, the two crystal forms were found in the same drop at pH 4.7. The differences in crystal packing in the two crystal forms can be explained by the pH-dependent variation in the protonation state of the glutamic acid residues on the protein surface. PubMed: 14993671DOI: 10.1107/S0907444903029767 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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