PDBe 1e2o

X-ray diffraction
3Å resolution

CATALYTIC DOMAIN FROM DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo 24-mer (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
Expression system: Escherichia coli
UniProt:
  • Canonical: NEW 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

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: F432
Unit cell:
a: 222.8Å b: 222.8Å c: 222.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.205 0.249
Expression system: Escherichia coli