2qmx

X-ray diffraction
2.3Å resolution

The crystal structure of L-Phe inhibited prephenate dehydratase from Chlorobium tepidum TLS

Released:

Function and Biology Details

Reaction catalysed:
Prephenate = phenylpyruvate + H(2)O + CO(2)
Biochemical function:
Cellular component:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-185105 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Prephenate dehydratase Chains: A, B
Molecule details ›
Chains: A, B
Length: 283 amino acids
Theoretical weight: 31.6 KDa
Source organism: Chlorobaculum tepidum TLS
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q8KBW6 (Residues: 1-280; Coverage: 100%)
Gene names: CT1666, pheA
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P21212
Unit cell:
a: 86.87Å b: 127.886Å c: 56.595Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.223 0.219 0.289
Expression system: Escherichia coli BL21