1JLL
Crystal Structure Analysis of the E197betaA Mutant of E. coli SCS
Summary for 1JLL
Entry DOI | 10.2210/pdb1jll/pdb |
Related | 1CQI 1CQJ 1EUC 1EUD 1JKJ 2SCU |
Descriptor | succinyl-CoA synthetase alpha subunit, succinyl-CoA synthetase beta subunit, PHOSPHATE ION, ... (6 entities in total) |
Functional Keywords | citric acid cycle, heterotetramer, ligase, atp-grasp fold, rossmann fold |
Biological source | Escherichia coli More |
Total number of polymer chains | 4 |
Total formula weight | 145763.73 |
Authors | Fraser, M.E. (deposition date: 2001-07-16, release date: 2002-01-30, Last modification date: 2023-08-16) |
Primary citation | Fraser, M.E.,Joyce, M.A.,Ryan, D.G.,Wolodko, W.T. Two glutamate residues, Glu 208 alpha and Glu 197 beta, are crucial for phosphorylation and dephosphorylation of the active-site histidine residue in succinyl-CoA synthetase. Biochemistry, 41:537-546, 2002 Cited by PubMed: 11781092DOI: 10.1021/bi011518y PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.69 Å) |
Structure validation
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