› 1i88

X-ray diffraction
1.45Å resolution

CHALCONE SYNTHASE (G256V)

Released:
DOI: 10.2210/pdb1i88/pdb
PDB entry 1i88 coloured by chain, front view.
PDB entry 1i88 coloured by chain, side view.
PDB entry 1i88 coloured by chain, top view.
Source organism: Medicago sativa
Primary publication:
Structure-guided programming of polyketide chain-length determination in chalcone synthase.
Jez JM, Bowman ME, Noel JP
Biochemistry 40 14829-38 (2001)
PMID: 11732902

Function and Biology Details

Reaction catalysed: 
3 malonyl-CoA + 4-coumaroyl-CoA = 4 CoA + naringenin chalcone + 3 CO(2)
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-151628 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chalcone synthase 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 389 amino acids
Theoretical weight: 42.83 KDa
Source organism: Medicago sativa
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P30074 (Residues: 1-389; Coverage: 100%)
Gene name: CHS2
Sequence domains:
Structure domains: Peroxisomal Thiolase; Chain A, domain 1

Ligands and Environments

1 bound ligand:
Ligand SO4 2 x SO4
1 modified residue:
Ligand CSD 2 x CSD

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P3121
Unit cell:
a: 98.292Å b: 98.292Å c: 129.676Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.197 0.203 0.221
Expression system: Escherichia coli BL21

Quick links

Citations

12 review citations

Structure and function of the chalcone synthase superfamily of plant type III polyketide synthases.
Abe et al. (2010)
11 more

1 mention without citation

On the evolutionary conservation of hydrogen bonds made by buried polar amino acids: the hidden joists, braces and trusses of protein architecture.
Worth et al. (2010)