› 1iax

X-ray diffraction
2.8Å resolution

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine = 1-aminocyclopropane-1-carboxylate + S-methyl-5'-thioadenosine
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-148386 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
1-aminocyclopropane-1-carboxylate synthase 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 428 amino acids
Theoretical weight: 48.29 KDa
Source organism: Solanum lycopersicum
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P18485 (Residues: 11-438; Coverage: 88%)
Gene names: ACC2, ACS2, PCVV4A
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 2 x PLP
1 bound ligand:
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P6422
Unit cell:
a: 123.2Å b: 123.2Å c: 212.8Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.218 0.218 0.293
Expression system: Escherichia coli BL21

Quick links

Citations

3 review citations

Eto Brute? Role of ACS turnover in regulating ethylene biosynthesis.
Chae et al. (2005)
2 more

1 mention without citation

Protein Phosphatases Type 2C Group A Interact with and Regulate the Stability of ACC Synthase 7 in Arabidopsis.
Marczak et al. (2020)