2nu6

X-ray diffraction
2.55Å resolution

C123aA Mutant of E. coli Succinyl-CoA Synthetase

Released:
Source organism: Escherichia coli
Primary publication:
Participation of Cys123alpha of Escherichia coli succinyl-CoA synthetase in catalysis.
Acta Crystallogr D Biol Crystallogr 63 876-84 (2007)
PMID: 17642514

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-141656 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Succinate--CoA ligase [ADP-forming] subunit alpha Chains: A, D
Molecule details ›
Chains: A, D
Length: 288 amino acids
Theoretical weight: 29.73 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AGE9 (Residues: 2-289; Coverage: 100%)
Gene names: JW0718, b0729, sucD
Sequence domains:
Structure domains:
Succinate--CoA ligase [ADP-forming] subunit beta Chains: B, E
Molecule details ›
Chains: B, E
Length: 388 amino acids
Theoretical weight: 41.44 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A836 (Residues: 1-388; Coverage: 100%)
Gene names: JW0717, b0728, sucC
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand COA 6 x COA
1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: P4322
Unit cell:
a: 97.22Å b: 97.22Å c: 386.56Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.196 0.247
Expression system: Escherichia coli