1xc4

X-ray diffraction
2.8Å resolution

Crystal structure of wild-type tryptophan synthase alpha-subunits from Escherichia coli

Released:
Source organism: Escherichia coli
Primary publication:
Structures of wild-type and P28L/Y173F tryptophan synthase alpha-subunits from Escherichia coli.
Biochem Biophys Res Commun 323 1257-64 (2004)
PMID: 15451433

Function and Biology Details

Reaction catalysed:
(1a) 1-C-(indol-3-yl)glycerol 3-phosphate = indole + D-glyceraldehyde 3-phosphate
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-141675 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tryptophan synthase alpha chain Chains: A, B
Molecule details ›
Chains: A, B
Length: 268 amino acids
Theoretical weight: 28.78 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A877 (Residues: 1-268; Coverage: 100%)
Gene names: JW1252, b1260, trpA
Sequence domains: Tryptophan synthase alpha chain
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: C2
Unit cell:
a: 162.273Å b: 44.479Å c: 71.519Å
α: 90° β: 106.56° γ: 90°
R-values:
R R work R free
0.305 0.244 0.318
Expression system: Escherichia coli