› 1rqh

X-ray diffraction
2Å resolution

Propionibacterium shermanii transcarboxylase 5S subunit bound to pyruvic acid

Released:
DOI: 10.2210/pdb1rqh/pdb
PDB entry 1rqh coloured by chain, front view.
PDB entry 1rqh coloured by chain, side view.
PDB entry 1rqh coloured by chain, top view.
Source organism: Propionibacterium freudenreichii subsp. shermanii
Primary publication:
Transcarboxylase 5S structures: assembly and catalytic mechanism of a multienzyme complex subunit.
Hall PR, Zheng R, Antony L, Pusztai-Carey M, Carey PR, Yee VC
EMBO J 23 3621-31 (2004)
PMID: 15329673

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180656 (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:
Ligand CO 1 x CO
Ligand PYR 1 x PYR
1 modified residue:
Ligand KCX 1 x KCX

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: C2221
Unit cell:
a: 96.025Å b: 145.72Å c: 78.747Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.166 0.164 0.197
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Structure, mechanism and regulation of pyruvate carboxylase.
Jitrapakdee et al. (2008)
8 more

1 mention without citation

Transcarboxylase 5S structures: assembly and catalytic mechanism of a multienzyme complex subunit.
Hall et al. (2004)