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1JLL

Crystal Structure Analysis of the E197betaA Mutant of E. coli SCS

Summary for 1JLL
Entry DOI10.2210/pdb1jll/pdb
Related1CQI 1CQJ 1EUC 1EUD 1JKJ 2SCU
Descriptorsuccinyl-CoA synthetase alpha subunit, succinyl-CoA synthetase beta subunit, PHOSPHATE ION, ... (6 entities in total)
Functional Keywordscitric acid cycle, heterotetramer, ligase, atp-grasp fold, rossmann fold
Biological sourceEscherichia coli
More
Total number of polymer chains4
Total formula weight145763.73
Authors
Fraser, M.E. (deposition date: 2001-07-16, release date: 2002-01-30, Last modification date: 2023-08-16)
Primary citationFraser, 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: 11781092
DOI: 10.1021/bi011518y
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.69 Å)
Structure validation

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