PDBe 1c4t

X-ray diffraction
3Å resolution

CATALYTIC DOMAIN FROM TRIMERIC DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 233 amino acids
Theoretical weight: 26.11 KDa
Source organism: Escherichia coli BL21(DE3)
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

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P3121
Unit cell:
a: 112.175Å b: 112.175Å c: 134.417Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.257 0.257 0.286
Expression system: Escherichia coli BL21(DE3)