6mel

X-ray diffraction
2.06Å resolution

Succinyl-CoA synthase from Campylobacter jejuni

Released:
Entry authors: Osipiuk J, Maltseva N, Jedrzejczak R, Satchell KJF, Joachimiak A, Center for Structural Genomics of Infectious Diseases (CSGID)

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-171046 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Succinate--CoA ligase [ADP-forming] subunit alpha Chain: A
Molecule details ›
Chain: A
Length: 295 amino acids
Theoretical weight: 30.85 KDa
Source organism: Campylobacter jejuni
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q0PAY2 (Residues: 1-289; Coverage: 100%)
Gene names: Cj0534, sucD
Sequence domains:
Structure domains:
Succinate--CoA ligase [ADP-forming] subunit beta Chain: B
Molecule details ›
Chain: B
Length: 387 amino acids
Theoretical weight: 41.8 KDa
Source organism: Campylobacter jejuni RM1221
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q5HVN3 (Residues: 1-387; Coverage: 100%)
Gene names: CJE0637, sucC
Sequence domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P3121
Unit cell:
a: 123.072Å b: 123.072Å c: 146.788Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.151 0.15 0.175
Expression system: Escherichia coli BL21(DE3)