› 1w9y

X-ray diffraction
2.1Å resolution

The structure of ACC oxidase

Released:
DOI: 10.2210/pdb1w9y/pdb
PDB entry 1w9y coloured by chain, front view.
PDB entry 1w9y coloured by chain, side view.
PDB entry 1w9y coloured by chain, top view.
Source organism: Petunia x hybrida
Primary publication:
Crystal structure and mechanistic implications of 1-aminocyclopropane-1-carboxylic acid oxidase--the ethylene-forming enzyme.
Zhang Z, Ren JS, Clifton IJ, Schofield CJ
Chem Biol 11 1383-94 (2004)
PMID: 15489165

Function and Biology Details

Reaction catalysed: 
1-aminocyclopropane-1-carboxylate + ascorbate + O(2) = ethylene + cyanide + dehydroascorbate + CO(2) + 2 H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170658 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
1-aminocyclopropane-1-carboxylate oxidase 1 Chain: A
Molecule details ›
Chain: A
Length: 319 amino acids
Theoretical weight: 36.94 KDa
Source organism: Petunia x hybrida
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q08506 (Residues: 1-319; Coverage: 100%)
Gene name: ACO1
Sequence domains:
Structure domains: B-lactam Antibiotic, Isopenicillin N Synthase; Chain

Ligands and Environments

1 bound ligand:
Ligand SO4 1 x SO4
1 modified residue:
Ligand MSE 15 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: I222
Unit cell:
a: 70.3Å b: 107.93Å c: 108.08Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.224 0.224 0.292
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

17 review citations

Recent advances in ethylene research.
Lin et al. (2009)
16 more

4 mentions without citation

Functional diversity of 2-oxoglutarate/Fe(II)-dependent dioxygenases in plant metabolism.
Farrow et al. (2014)
3 more