1scz

X-ray diffraction
2.2Å resolution

Improved structural model for the catalytic domain of E.coli dihydrolipoamide succinyltransferase

Released:
Source organism: Escherichia coli K-12
Entry authors: Schormann N, Symersky J, Carson M, Luo M, Tsao J, Johnson D, Huang W-Y, Pruett P, Lin G, Li S, Qiu S, Arabashi A, Bunzel B, Luo D, Nagy L, Gray R, Luan C-H, Zhang Z, Lu S, DeLucas L

Function and Biology Details

Reaction catalysed:
Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-succinyldihydrolipoyl)lysine
Biochemical function:
Biological process:

Structure analysis Details

Assembly composition:
homo 24-mer (preferred)
PDBe Complex ID:
PDB-CPX-142720 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex Chain: A
Molecule details ›
Chain: A
Length: 233 amino acids
Theoretical weight: 26.11 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0AFG6 (Residues: 173-405; Coverage: 58%)
Gene names: JW0716, b0727, sucB
Sequence domains: 2-oxoacid dehydrogenases acyltransferase (catalytic domain)
Structure domains: Chloramphenicol acetyltransferase-like domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: F432
Unit cell:
a: 220.576Å b: 220.576Å c: 220.576Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.211 0.234
Expression system: Escherichia coli BL21(DE3)