PDBe 1geq

X-ray diffraction
2Å resolution

Entropic stabilization of the tryptophan synthase A-subunit from a hyperthermophile, pyrococcus furiosus: X-ray analysis and calorimetry

Released:

Function and Biology Details

Reaction catalysed:
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H(2)O. 
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tryptophan synthase alpha chain Chains: A, B
Molecule details ›
Chains: A, B
Length: 248 amino acids
Theoretical weight: 27.54 KDa
Source organism: Pyrococcus furiosus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8U094 (Residues: 1-248; Coverage: 100%)
Gene names: PF1705, trpA
Sequence domains: Tryptophan synthase alpha chain
Structure domains: Aldolase class I

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-18B
Spacegroup: C2221
Unit cell:
a: 73.013Å b: 78.997Å c: 170.964Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.198 0.249
Expression system: Escherichia coli