1URR
A novel Drosophila Melanogaster Acylphosphatase (AcPDro2)
Summary for 1URR
| Entry DOI | 10.2210/pdb1urr/pdb |
| Descriptor | CG18505 PROTEIN, GLYCEROL (3 entities in total) |
| Functional Keywords | acylphosphatase, enzyme, hydrolase |
| Biological source | DROSOPHILA MELANOGASTER (FRUIT FLY) |
| Total number of polymer chains | 1 |
| Total formula weight | 11875.63 |
| Authors | Rosano, C.,Zuccotti, S.,Bolognesi, M. (deposition date: 2003-11-03, release date: 2004-05-27, Last modification date: 2023-12-13) |
| Primary citation | Zuccotti, S.,Rosano, C.,Ramazzotti, M.,Degl'Innocenti, D.,Stefani, M.,Manao, G.,Bolognesi, M. Three-Dimensional Structural Characterization of a Novel Drosophila Melanogaster Acylphosphatase Acta Crystallogr.,Sect.D, 60:1177-, 2004 Cited by PubMed Abstract: Analysis of the Drosophila melanogaster EST database led to the discovery and cloning of a novel acylphosphatase. The CG18505 gene coding for a new enzyme (AcPDro2) is clearly distinct from the previously described CG16870Acyp gene, which also codes for a D. melanogaster acylphosphatase (AcPDro). The putative catalytic residues, together with residues held to stabilize the acylphosphatase fold, are conserved in the two encoded proteins. Crystals of AcPDro2, which belong to the trigonal space group P3(1)21, with unit-cell parameters a = b = 45.8, c = 98.6 angstroms, gamma = 120 degrees, allowed the solution of the protein structure by molecular replacement and its refinement to 1.5 angstroms resolution. The AcPDro2 active-site structure is discussed. PubMed: 15159593DOI: 10.1107/S0907444904006808 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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