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-Structure paper
| Title | 240s Loop Interactions Stabilize the T State of Escherichia coli Aspartate Transcarbamoylase. |
|---|---|
| Journal, issue, pages | J. Biol. Chem., Vol. 279, Page 23302-23310, Year 2004 |
| Publish date | Mar 5, 2004 (structure data deposition date) |
Authors | Alam, N. / Stieglitz, K.A. / Caban, M.D. / Gourinath, S. / Tsuruta, H. / Kantrowitz, E.R. |
External links | J. Biol. Chem. / PubMed:15014067 |
| Methods | X-ray diffraction |
| Resolution | 2.6 Å |
| Structure data | ![]() PDB-1sku: |
| Chemicals | ![]() ChemComp-MLI: ![]() ChemComp-ZN: ![]() ChemComp-HOH: |
| Source |
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Keywords | TRANSFERASE / allosteric enzyme / loop movements / small-angle X-ray scattering / domain closure / allosteric transition / intersubunit interactions |
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