X-ray diffraction
1.55Å resolution

Crystal structure of Synechocystis arogenate dehydrogenase


Function and Biology Details

Reaction catalysed:
L-arogenate + NAD(+) = L-tyrosine + NADH + CO(2)
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Prephenate/arogenate dehydrogenase domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 279 amino acids
Theoretical weight: 30.32 KDa
Source organism: Synechocystis sp. PCC 6803
Expression system: Escherichia coli
  • Canonical: P73906 (Residues: 1-279; Coverage: 100%)
Gene name: tyrA
Sequence domains:
Structure domains:

Ligands and Environments

Cofactor: Ligand NAP 4 x NAP
1 bound ligand:
2 modified residues:

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4, null
Spacegroup: P21
Unit cell:
a: 66.15Å b: 70.85Å c: 104.49Å
α: 90° β: 90.3° γ: 90°
R R work R free
0.19 0.189 0.222
Expression system: Escherichia coli