› 1b8g

X-ray diffraction
2.37Å resolution

1-AMINOCYCLOPROPANE-1-CARBOXYLATE SYNTHASE

Released:
DOI: 10.2210/pdb1b8g/pdb
PDB entry 1b8g coloured by chain, front view.
PDB entry 1b8g coloured by chain, side view.
PDB entry 1b8g coloured by chain, top view.
Source organism: Malus domestica
Primary publication:
Structure of 1-aminocyclopropane-1-carboxylate synthase, a key enzyme in the biosynthesis of the plant hormone ethylene.
Capitani G, Hohenester E, Feng L, Storici P, Kirsch JF, Jansonius JN
J Mol Biol 294 745-56 (1999)
PMID: 10610793

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-153493 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
1-aminocyclopropane-1-carboxylate synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 429 amino acids
Theoretical weight: 48.26 KDa
Source organism: Malus domestica
Expression system: Escherichia coli
UniProt:
  • Canonical: P37821 (Residues: 3-431; Coverage: 91%)
Gene name: ACS-1
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 2 x PLP
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELLIOTT GX-20
Spacegroup: P21
Unit cell:
a: 53.63Å b: 69.06Å c: 123.24Å
α: 90° β: 90.04° γ: 90°
R-values:
R R work R free
0.179 0.179 0.242
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Ethylene biosynthesis and signaling networks.
Wang et al. (2002)
8 more

7 mentions without citation

Natural history of S-adenosylmethionine-binding proteins.
Kozbial et al. (2005)
6 more