2nu9

X-ray diffraction
2.9Å resolution

C123aT Mutant of E. coli Succinyl-CoA Synthetase Orthorhombic Crystal Form

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)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Succinate--CoA ligase [ADP-forming] subunit alpha Chains: A, D, F, H
Molecule details ›
Chains: A, D, F, H
Length: 288 amino acids
Theoretical weight: 29.76 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, G, I
Molecule details ›
Chains: B, E, G, I
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
1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: P212121
Unit cell:
a: 98.53Å b: 154.9Å c: 240.62Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.23 0.229 0.251
Expression system: Escherichia coli