PDBe 2dzp

X-ray diffraction
2.4Å resolution

Structure of mutant tryptophan synthase alpha-subunit (D17N) from a hyperthermophile, Pyrococcus furiosus

Source organism: Pyrococcus furiosus
Entry authors: Ogasahara K, Yamagata Y, Yutani K, RIKEN Structural Genomics/Proteomics Initiative (RSGI)

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
Tryptophan synthase alpha chain Chains: A, B
Molecule details ›
Chains: A, B
Length: 248 amino acids
Theoretical weight: 27.53 KDa
Source organism: Pyrococcus furiosus
Expression system: Escherichia coli
  • 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: SPRING-8 BEAMLINE BL40B2
Spacegroup: C2221
Unit cell:
a: 74.268Å b: 75.777Å c: 165.869Å
α: 90° β: 90° γ: 90°
R R work R free
0.218 0.218 0.279
Expression system: Escherichia coli