1XOY
Solution structure of At3g04780.1, an Arabidopsis ortholog of the C-terminal domain of human thioredoxin-like protein
Summary for 1XOY
| Entry DOI | 10.2210/pdb1xoy/pdb |
| NMR Information | BMRB: 6341 |
| Descriptor | hypothetical protein At3g04780.1 (1 entity in total) |
| Functional Keywords | structural genomics, protein structure initiative, center for eukaryotic structural genomics, psi, cesg, unknown function |
| Biological source | Arabidopsis thaliana (thale cress) |
| Total number of polymer chains | 1 |
| Total formula weight | 17918.00 |
| Authors | Song, J.,Robert, C.T.,Lee, M.S.,Markley, J.L.,Center for Eukaryotic Structural Genomics (CESG) (deposition date: 2004-10-07, release date: 2004-10-12, Last modification date: 2024-05-22) |
| Primary citation | Song, J.,Tyler, R.C.,Wrobel, R.L.,Frederick, R.O.,Vojtek, F.C.,Jeon, W.B.,Lee, M.S.,Markley, J.L. Solution structure of At3g04780.1-des15, an Arabidopsis thaliana ortholog of the C-terminal domain of human thioredoxin-like protein. Protein Sci., 14:1059-1063, 2005 Cited by PubMed Abstract: The structure of At3g04780.1-des15, an Arabidopsis thaliana ortholog of the C-terminal domain of human thioredoxin-like protein, was determined by NMR spectroscopy. The structure is dominated by a beta-barrel sandwich. A two-stranded anti-parallel beta-sheet, which seals off one end of the beta-barrel, is flanked by two flexible loops rich in acidic amino acids. Although this fold often provides a ligand binding site, the structure did not reveal an appreciable cavity inside the beta-barrel. The three-dimensional structure of At3g04780.1-des15 provides an entry point for understanding its functional role and those of its mammalian homologs. PubMed: 15741346DOI: 10.1110/ps.041246805 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
