4FWU
Crystal structure of glutaminyl cyclase from drosophila melanogaster in space group I4
Summary for 4FWU
| Entry DOI | 10.2210/pdb4fwu/pdb |
| Related | 4F9U 4F9V |
| Descriptor | CG32412, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ZINC ION, ... (6 entities in total) |
| Functional Keywords | alpha/beta hydrolase, pglu formation, alzheimer`s disease, pyroglutamate, pglu-amyloid, glycosylation, hydrolase |
| Biological source | Drosophila melanogaster (Fruit fly) |
| Total number of polymer chains | 1 |
| Total formula weight | 36660.14 |
| Authors | Kolenko, P.,Koch, B.,Stubbs, M.T. (deposition date: 2012-07-02, release date: 2012-09-05, Last modification date: 2024-11-06) |
| Primary citation | Kolenko, P.,Koch, B.,Rahfeld, J.U.,Schilling, S.,Demuth, H.U.,Stubbs, M.T. Structure of glutaminyl cyclase from Drosophila melanogaster in space group I4. Acta Crystallogr.,Sect.F, 69:358-361, 2013 Cited by PubMed Abstract: The structure of ligand-free glutaminyl cyclase (QC) from Drosophila melanogaster (DmQC) has been determined in a novel crystal form. The protein crystallized in space group I4, with unit-cell parameters a = b = 122.3, c = 72.7 Å. The crystal diffracted to a resolution of 2 Å at the home source. The structure was solved by molecular replacement and was refined to an R factor of 0.169. DmQC exhibits a typical α/β-hydrolase fold. The electron density of three monosaccharides could be localized. The accessibility of the active site will facilitate structural studies of novel inhibitor-binding modes. PubMed: 23545638DOI: 10.1107/S1744309113005575 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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