4NT4
Crystal structure of the kinase domain of Gilgamesh isoform I from Drosophila melanogaster
Summary for 4NT4
| Entry DOI | 10.2210/pdb4nt4/pdb |
| Descriptor | Gilgamesh, isoform I, SULFATE ION, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | serine/threonine protein kinase, wnt signaling pathway, transferase |
| Biological source | Drosophila melanogaster (Fruit fly) |
| Total number of polymer chains | 1 |
| Total formula weight | 36706.27 |
| Authors | Chen, C.C.,Shi, Z.B.,Zhou, Z.C. (deposition date: 2013-11-30, release date: 2014-04-09, Last modification date: 2023-11-08) |
| Primary citation | Han, N.,Chen, C.,Shi, Z.,Cheng, D. Structure of the kinase domain of Gilgamesh from Drosophila melanogaster Acta Crystallogr.,Sect.F, 70:438-443, 2014 Cited by PubMed Abstract: The CK1 family kinases regulate multiple cellular aspects and play important roles in Wnt/Wingless and Hedgehog signalling. The kinase domain of Drosophila Gilgamesh isoform I (Gilgamesh-I), a homologue of human CK1-γ, was purified and crystallized. Crystals of methylated Gilgamesh-I kinase domain with a D210A mutation diffracted to 2.85 Å resolution and belonged to space group P43212, with unit-cell parameters a = b = 52.025, c = 291.727 Å. The structure of Gilgamesh-I kinase domain, which was determined by molecular replacement, has conserved catalytic elements and an active conformation. Structural comparison indicates that an extended loop between the α1 helix and the β4 strand exists in the Gilgamesh-I kinase domain. This extended loop may regulate the activity and function of Gilgamesh-I. PubMed: 24699734DOI: 10.1107/S2053230X14004774 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.86 Å) |
Structure validation
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