1rr2

X-ray diffraction
2Å resolution

Propionibacterium shermanii transcarboxylase 5S subunit bound to 2-ketobutyric acid

Released:

Function and Biology Details

Reaction catalysed:
(S)-methylmalonyl-CoA + pyruvate = propanoyl-CoA + oxaloacetate
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methylmalonyl-CoA carboxyltransferase 5S subunit Chain: A
Molecule details ›
Chain: A
Length: 539 amino acids
Theoretical weight: 59.65 KDa
Source organism: Propionibacterium freudenreichii subsp. shermanii
Expression system: Escherichia coli
UniProt:
  • Canonical: Q70AC7 (Residues: 2-505; Coverage: 100%)
Sequence domains:
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: C2221
Unit cell:
a: 96.172Å b: 146.134Å c: 78.701Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.173 0.205
Expression system: Escherichia coli