5DK8
Human ubiquitin in the P1 space group
Summary for 5DK8
| Entry DOI | 10.2210/pdb5dk8/pdb |
| Descriptor | Polyubiquitin-B, MAGNESIUM ION (3 entities in total) |
| Functional Keywords | signaling protein |
| Biological source | Homo sapiens (Human) |
| Cellular location | Ubiquitin: Cytoplasm : P0CG47 |
| Total number of polymer chains | 2 |
| Total formula weight | 17354.06 |
| Authors | Camara-Artigas, A.,Bacarizo, J. (deposition date: 2015-09-03, release date: 2015-12-16, Last modification date: 2024-01-10) |
| Primary citation | Camara-Artigas, A.,Plaza-Garrido, M.,Martinez-Rodriguez, S.,Bacarizo, J. New crystal form of human ubiquitin in the presence of magnesium. Acta Crystallogr.,Sect.F, 72:29-35, 2016 Cited by PubMed Abstract: Ubiquitin is a small globular protein that has a considerable number of lysine residues on its surface. This results in a high surface entropy that precludes the formation of crystal-packing interactions. To date, only a few structures of the native form of ubiquitin have been solved, and most of the crystals that led to these structures were obtained in the presence of different divalent metal cations. In this work, a new crystallographic structure of human ubiquitin solved from crystals grown in the presence of magnesium is presented. The crystals belonged to a triclinic space group, with unit-cell parameters a = 29.96, b = 30.18, c = 41.41 Å, α = 88.52, β = 79.12, γ = 67.37°. The crystal lattice is composed of stacked layers of human ubiquitin molecules with a large hydrophobic interface and a smaller polar interface in which the magnesium ion lies at the junction between adjacent layers in the crystal. The metal ion appears in a hexa-aquo coordination, which is key to facilitating the crystallization of the protein. PubMed: 26750481DOI: 10.1107/S2053230X15023390 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.32 Å) |
Structure validation
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