2nua

X-ray diffraction
2.95Å resolution

C123aV 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: 29.68 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 4 x COA
2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P4322
Unit cell:
a: 97.51Å b: 97.51Å c: 390.25Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.226 0.221 0.264
Expression system: Escherichia coli