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PDBe Entry: 1jll 
Crystal Structure Analysis of the E197betaA Mutant of E. coli SCS
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LIGASE
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X-RAY DIFFRACTION
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Resolution: 2.69 Å, R-factor: 22.3%, Free R-factor: 25.9%, Spacegroup: P 43 2 2
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30/01/2002, deposition: 16/07/2001, last revision: 24/02/2009
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Fraser, M.E.
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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 vol:41, pag:537-546 (2002) [PubMed ID 11781092 ]
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CITRIC ACID CYCLE, HETEROTETRAMER, LIGASE, ATP-GRASP FOLD, ROSSMANN FOLD
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6.2.1.5 ExPASy BRENDA (A B D E)
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Escherichia coli 562(A D B E)
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Succinyl-CoA ligase [ADP-forming] subunit alpha (EC 6.2.1.5) (Succinyl-CoA synthetase subunit alpha) (SCS-alpha) P0AGF1 (A D)
Succinyl-CoA ligase [ADP-forming] subunit beta (EC 6.2.1.5) (Succinyl-CoA synthetase subunit beta) (SCS-beta) P0A836 (B E)
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A, B, D, E
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1jkj, 2scu, 1cqi, 1cqj, 1euc, 1eud
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| A, D |
succinyl-CoA synthetase alpha subunit |
Protein |
P0AGF1 (SUCD_ECO57)
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288 |
99% |
| B, E |
succinyl-CoA synthetase beta subunit |
Protein |
P0A836 (SUCC_ECOLI)
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388 |
100% |
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| A, D |
PHOSPHATE ION |
PO4
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| B, E |
SULFATE ION |
SO4
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| A, D, B, E |
COENZYME A |
COA
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