Summary for 1XOB
| Entry DOI | 10.2210/pdb1xob/pdb |
| Descriptor | THIOREDOXIN (1 entity in total) |
| Functional Keywords | electron transport, redox-active center |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 11687.39 |
| Authors | Jeng, M.-F.,Campbell, A.P.,Begley, T.,Holmgren, A.,Case, D.A.,Wright, P.E.,Dyson, H.J. (deposition date: 1995-11-28, release date: 1996-06-10, Last modification date: 2024-05-01) |
| Primary citation | Jeng, M.F.,Campbell, A.P.,Begley, T.,Holmgren, A.,Case, D.A.,Wright, P.E.,Dyson, H.J. High-resolution solution structures of oxidized and reduced Escherichia coli thioredoxin. Structure, 2:853-868, 1994 Cited by PubMed Abstract: Thioredoxin participates in thiol-disulfide exchange reactions and both oxidized thioredoxin (disulfide form) and reduced thioredoxin (dithiol form) are found under physiological conditions. Previous structural studies suggested that the two forms were extremely similar, although significant functional and spectroscopic differences exist. We therefore undertook high-resolution solution structural studies of the two forms of Escherichia coli thioredoxin in order to detect subtle conformational differences. PubMed: 7812718DOI: 10.1016/S0969-2126(94)00086-7 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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