X-ray diffraction
2Å resolution

Crystal structure of apo C298S tryptophanase from E.coli


Function and Biology Details

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Tryptophanase Chain: A
Molecule details ›
Chain: A
Length: 467 amino acids
Theoretical weight: 52.37 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
  • Canonical: P0A853 (Residues: 5-471; Coverage: 99%)
Gene names: JW3686, b3708, ind, tnaA
Sequence domains: Beta-eliminating lyase
Structure domains:

Ligands and Environments

2 bound ligands:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: F222
Unit cell:
a: 120.484Å b: 118.77Å c: 171.534Å
α: 90° β: 90° γ: 90°
R R work R free
0.215 0.215 0.257
Expression system: Escherichia coli