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-Structure paper
Title | Crystal structure of the thioesterification conformation of Bacillus subtilis o-succinylbenzoyl-CoA synthetase reveals a distinct substrate-binding mode |
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Journal, issue, pages | J. Biol. Chem., Vol. 292, Page 12296-12310, Year 2017 |
Publish date | Mar 2, 2017 (structure data deposition date) |
![]() | Chen, Y. / Li, T.L. / Lin, X. / Li, X. / Li, X.D. / Guo, Z. |
![]() | ![]() ![]() |
Methods | X-ray diffraction |
Resolution | 1.763 - 1.9 Å |
Structure data | ![]() PDB-5x8f: ![]() PDB-5x8g: |
Chemicals | ![]() ChemComp-S0N: ![]() ChemComp-AMP: ![]() ChemComp-MG: ![]() ChemComp-NA: ![]() ChemComp-PEG: ![]() ChemComp-CA: ![]() ChemComp-HOH: |
Source |
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![]() | LIGASE / Adenylate-forming Enzyme / acyl-CoA synthetase / thioester conformation / CoA / pantetheine tunnel / ADP binding subsite / domain alternation / large conformational change / inter-domain linker |