› 5ie3

X-ray diffraction
1.9Å resolution

Crystal structure of a plant enzyme

Released:
DOI: 10.2210/pdb5ie3/pdb
PDB entry 5ie3 coloured by chain, front view.
PDB entry 5ie3 coloured by chain, side view.
PDB entry 5ie3 coloured by chain, top view.
Source organism: Arabidopsis thaliana
Primary publication:
Crystal Structures of Arabidopsis thaliana Oxalyl-CoA Synthetase Essential for Oxalate Degradation.
Fan M, Xiao Y, Li M, Chang W
Mol Plant 9 1349-1352 (2016)
PMID: 27326693

Function and Biology Details

Reaction catalysed: 
ATP + oxalate + CoA = AMP + diphosphate + oxalyl-CoA
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193488 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Oxalate--CoA ligase Chains: A, B
Molecule details ›
Chains: A, B
Length: 514 amino acids
Theoretical weight: 55.61 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9SMT7 (Residues: 1-514; Coverage: 100%)
Gene names: 4CLL10, AAE3, AMPBP3, At3g48990, T2J13.170
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand AMP 2 x AMP
Ligand OXD 2 x OXD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P21
Unit cell:
a: 71.193Å b: 117.043Å c: 72.062Å
α: 90° β: 93.59° γ: 90°
R-values:
R R work R free
0.161 0.16 0.206
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

FoldAffinity: binding affinities from nDSF experiments.
Niebling et al. (2021)
1 more

1 mention without citation

The identification and characterization of an oxalyl-CoA synthetase from grass pea (Lathyrus sativus L.).
Goldsmith et al. (2022)