1AIE
P53 TETRAMERIZATION DOMAIN CRYSTAL STRUCTURE
Summary for 1AIE
| Entry DOI | 10.2210/pdb1aie/pdb |
| Descriptor | P53 (2 entities in total) |
| Functional Keywords | p53 tetramerization, oligomer, dna, transcription, tumor suppressor |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm. Isoform 1: Nucleus. Isoform 2: Nucleus. Isoform 3: Nucleus. Isoform 4: Nucleus. Isoform 7: Nucleus. Isoform 8: Nucleus. Isoform 9: Cytoplasm: P04637 |
| Total number of polymer chains | 1 |
| Total formula weight | 3766.22 |
| Authors | Mittl, P.R.E.,Chene, P.,Gruetter, M.G. (deposition date: 1997-04-17, release date: 1997-06-16, Last modification date: 2024-05-22) |
| Primary citation | Mittl, P.R.,Chene, P.,Grutter, M.G. Crystallization and structure solution of p53 (residues 326-356) by molecular replacement using an NMR model as template. Acta Crystallogr.,Sect.D, 54:86-89, 1998 Cited by PubMed Abstract: The molecular replacement method is a powerful technique for crystal structure solution but the use of NMR structures as templates often causes problems. In this work the NMR structure of the p53 tetramerization domain has been used to solve the crystal structure by molecular replacement. Since the rotation- and translation-functions were not sufficiently clear, additional information about the symmetry of the crystal and the protein complex was used to identify correct solutions. The three-dimensional structure of residues 326-356 was subsequently refined to a final R factor of 19.1% at 1.5 A resolution. PubMed: 9761820DOI: 10.1107/S0907444997006550 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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