1QZU
crystal structure of human phosphopantothenoylcysteine decarboxylase
Summary for 1QZU
| Entry DOI | 10.2210/pdb1qzu/pdb |
| Descriptor | hypothetical protein MDS018, FLAVIN MONONUCLEOTIDE (2 entities in total) |
| Functional Keywords | alpha-beta sandwich, lyase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 4 |
| Total formula weight | 92090.66 |
| Authors | Manoj, N.,Ealick, S.E. (deposition date: 2003-09-17, release date: 2004-03-23, Last modification date: 2024-11-13) |
| Primary citation | Manoj, N.,Ealick, S.E. Unusual space-group pseudosymmetry in crystals of human phosphopantothenoylcysteine decarboxylase. Acta Crystallogr.,Sect.D, 59:1762-1766, 2003 Cited by PubMed Abstract: Phosphopantothenoylcysteine (PPC) decarboxylase is an essential enzyme in the biosynthesis of coenzyme A and catalyzes the decarboxylation of PPC to phosphopantetheine. Human PPC decarboxylase has been expressed in Escherichia coli, purified and crystallized. The Laue class of the diffraction data appears to be 3m, suggesting space group R32 with two monomers per asymmetric unit. However, the crystals belong to the space group R3 and the asymmetric unit contains four monomers. The structure has been solved using molecular replacement and refined to a current R factor of 29%. The crystal packing can be considered as two interlaced lattices, each consistent with space group R32 and with the corresponding twofold axes parallel to each other but separated along the threefold axis. Thus, the true space group is R3 with four monomers per asymmetric unit. PubMed: 14501115DOI: 10.1107/S0907444903016214 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.91 Å) |
Structure validation
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