› 1vgq

X-ray diffraction
2.13Å resolution

Formyl-CoA transferase mutant Asp169 to Ala

Released:
DOI: 10.2210/pdb1vgq/pdb
PDB entry 1vgq coloured by chain, front view.
PDB entry 1vgq coloured by chain, side view.
PDB entry 1vgq coloured by chain, top view.
Source organism: Oxalobacter formigenes
Primary publication:
Kinetic and mechanistic characterization of the formyl-CoA transferase from Oxalobacter formigenes.
Jonsson S, Ricagno S, Lindqvist Y, Richards NG
J Biol Chem 279 36003-12 (2004)
PMID: 15213226

Function and Biology Details

Reaction catalysed: 
Formyl-CoA + oxalate = formate + oxalyl-CoA
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-126525 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Formyl-CoA:oxalate CoA-transferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 427 amino acids
Theoretical weight: 47.19 KDa
Source organism: Oxalobacter formigenes
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O06644 (Residues: 2-428; Coverage: 100%)
Gene name: frc
Sequence domains: CoA-transferase family III
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand CAO 2 x CAO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: I4
Unit cell:
a: 151.116Å b: 151.116Å c: 99.593Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.172 0.171 0.202
Expression system: Escherichia coli BL21(DE3)

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Citations

4 review citations

The enzymes of oxalate metabolism: unexpected structures and mechanisms.
Svedruzić et al. (2005)
3 more