› 1q6y

X-ray diffraction
1.99Å resolution

Hypothetical protein YfdW from E. coli bound to Coenzyme A

Released:
DOI: 10.2210/pdb1q6y/pdb
PDB entry 1q6y coloured by chain, front view.
PDB entry 1q6y coloured by chain, side view.
PDB entry 1q6y coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structure of Escherichia coli YfdW, a type III CoA transferase.
Gogos A, Gorman J, Shapiro L
Acta Crystallogr D Biol Crystallogr 60 507-11 (2004)
PMID: 14993676

Function and Biology Details

Reaction catalysed: 
Formyl-CoA + oxalate = formate + oxalyl-CoA
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159681 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Formyl-CoA:oxalate CoA-transferase Chain: A
Molecule details ›
Chain: A
Length: 428 amino acids
Theoretical weight: 47.24 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P69902 (Residues: 2-416; Coverage: 100%)
Gene names: JW2371, b2374, frc, yfdW
Sequence domains: CoA-transferase family III
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand COA 1 x COA
Ligand MPD 7 x MPD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 31-ID
Spacegroup: C2
Unit cell:
a: 92.117Å b: 66.779Å c: 73.049Å
α: 90° β: 108.73° γ: 90°
R-values:
R R work R free
0.17 0.16 0.2
Expression system: Escherichia coli

Quick links

Citations

1 review citation

The enzymes of oxalate metabolism: unexpected structures and mechanisms.
Svedruzić et al. (2005)
8 other articles

2 mentions without citation

Formyl-coenzyme A (CoA):oxalate CoA-transferase from the acidophile Acetobacter aceti has a distinctive electrostatic surface and inherent acid stability.
Mullins et al. (2012)
1 more